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	<title>Creative Biolabs Therapeutic Glycoprotein Blog</title>
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	<title>Creative Biolabs Therapeutic Glycoprotein Blog</title>
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		<title>The Intricate World of Glycoprotein Synthesis: Unraveling Key Mechanisms and Applications</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/glycoprotein-synthesismechanisms-applications/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Fri, 25 Oct 2024 03:24:54 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<category><![CDATA[Glycoprotein]]></category>
		<category><![CDATA[Glycoprotein Synthesis]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=55</guid>

					<description><![CDATA[Glycoproteins are essential biomolecules that perform a variety of functions across cellular systems, including structural roles, enzymatic activities, signaling pathways, and immune defense mechanisms. Central to glycoprotein functionality is glycosylation, the attachment<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/glycoprotein-synthesismechanisms-applications/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p>Glycoproteins are essential biomolecules that perform a variety of functions across cellular systems, including structural roles, enzymatic activities, signaling pathways, and immune defense mechanisms. Central to glycoprotein functionality is <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycosylation-of-therapeutic-protein.htm">glycosylation</a></span>, the attachment of sugar molecules to proteins. Glycosylation not only impacts protein folding and stability but also influences biological activities such as cellular interactions and recognition processes. This article will delve into the synthesis of glycoproteins, focusing on the biochemical processes, types of glycosylation, and applications in biotechnology.</p>
<p><strong>Cellular Machinery Driving Glycoprotein Synthesis</strong></p>
<p><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycoprotein-synthesis.htm">Glycoprotein synthesis</a> </span>involves complex enzymatic processes that occur within various cellular compartments. Two primary types of glycosylation play pivotal roles in glycoprotein formation: N-linked glycosylation and O-linked glycosylation. Both types begin after the protein is synthesized on ribosomes bound to the rough endoplasmic reticulum (ER). However, these glycosylation types follow distinct pathways and add unique glycan structures to proteins.</p>
<p><strong>N-linked Glycosylation</strong></p>
<p><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-n-linked-oligosaccharide-synthesis.htm">N-linked glycosylation</a> </span>involves the covalent attachment of oligosaccharides to asparagine residues within specific amino acid sequences. This process starts in the ER, where a lipid-linked oligosaccharide (LLO) precursor is constructed on the cytoplasmic face of the ER membrane. Through a process called &#8220;flipping,&#8221; the oligosaccharide is transferred into the ER lumen for further modification.</p>
<p>A key enzyme, oligosaccharyltransferase (OST), catalyzes the transfer of the oligosaccharide from the lipid anchor to nascent proteins, specifically targeting the asparagine residue within the consensus sequence (Asn-X-Ser/Thr). Following this, glycoproteins undergo folding, quality control, and initial trimming of the attached glycans within the ER. Proteins with improper folding structures are flagged for degradation, while correctly folded glycoproteins are transferred to the Golgi apparatus for additional modifications.</p>
<p>The Golgi apparatus serves as a processing hub, refining and diversifying the glycan structures of glycoproteins. Depending on the pathway, N-glycans may develop into high-mannose, hybrid, or complex forms, each conferring distinct functional properties to the protein.</p>
<p><strong>O-linked Glycosylation: Tailoring Proteins with Flexibility</strong></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/biosynthesis-of-o-linked-glycoproteins.htm"><span style="color: #0000ff;">O-linked glycosylation</span></a> occurs predominantly in the Golgi apparatus and involves the attachment of sugars to serine or threonine residues on proteins. Unlike N-linked glycosylation, O-linked glycosylation does not follow a rigid consensus sequence. Instead, glycosyltransferase enzymes attach N-acetylgalactosamine (GalNAc) directly to the hydroxyl groups of amino acids, with additional monosaccharides added to extend the glycan structure.</p>
<p>This form of glycosylation is particularly abundant in mucin-type glycoproteins, which are known for their role in forming protective barriers on epithelial surfaces. These glycoproteins contribute to the viscosity of mucus, an essential feature for protecting tissues in the respiratory, digestive, and reproductive systems.</p>
<p><strong>Biological Significance of Glycosylation in Glycoproteins</strong></p>
<p>Glycosylation affects numerous aspects of glycoprotein behavior, such as stability, solubility, folding efficiency, and recognition by other biomolecules. For example, glycosylation plays a critical role in immune responses by modulating the activity of antibodies and cell-surface receptors. Immunoglobulins, which are essential to the body&#8217;s defense mechanisms, rely on specific glycan structures to maintain their functional conformation and mediate interactions with immune cells.</p>
<p>Therapeutic proteins also require precise glycosylation to achieve their intended biological activity. A well-known example is erythropoietin (EPO), a glycoprotein hormone used to treat anemia. The addition of specific glycan structures is essential for EPO’s proper folding, stability, and biological half-life in circulation.</p>
<p>However, disruptions in glycosylation pathways can lead to congenital disorders of glycosylation (CDGs), which cause severe metabolic and developmental abnormalities. This underscores the importance of glycan structures in maintaining healthy physiological functions.</p>
<p><strong>Advances in Biotechnological Applications of Glycoproteins</strong></p>
<p>In recent decades, the synthesis and engineering of glycoproteins have become increasing important in biotechnology and pharmaceutical research. <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-production-in-mammalian-cells.htm">Recombinant glycoprotein production</a></span> is now a cornerstone of therapeutic protein development, particularly in the biopharmaceutical industry. Expression systems such as Chinese hamster ovary (CHO) cells and yeast are commonly used to produce glycoproteins with consistent glycan profiles. These systems are optimized for scalability and precise glycosylation patterns, ensuring that therapeutic proteins meet regulatory standards.</p>
<p><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoengineering-service.htm">Glycoengineering</a></span>—the manipulation of glycan structures—offers exciting possibilities for enhancing therapeutic proteins. For instance, monoclonal antibodies with modified glycan profiles demonstrate improved antibody-dependent cellular cytotoxicity (ADCC), a property that enhances their effectiveness in cancer treatment. In therapeutic antibody development, reducing the fucosylation of glycan structures has been shown to enhance binding affinity for immune effector cells.</p>
<p>Site-specific glycosylation technologies have also emerged, enabling precise control over glycan attachment. By manipulating the glycosylation sites of therapeutic proteins, researchers can fine-tune their stability and interaction with biological targets, paving the way for next-generation biologics.</p>
<p><strong>Challenges in Glycoprotein Synthesis and Analytical Strategies</strong></p>
<p>Despite significant advancements in glycoprotein synthesis, challenges remain in achieving consistent <a href="https://www.creative-biolabs.com/glycoprotein/glycan-profiling.htm"><span style="color: #0000ff;">glycan profiles</span></a> across production batches. The heterogeneity of glycan structures poses a significant obstacle, as even slight variations can impact the biological activity of <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-development.htm">therapeutic glycoproteins</a></span>. To address this, researchers employ analytical techniques such as mass spectrometry (MS) and liquid chromatography to characterize glycan profiles.</p>
<p>However, there is still room for improvement in the resolution and sensitivity of these analytical methods. Developing more robust glycoprotein analysis tools will be essential for future research and quality control in biopharmaceutical manufacturing.</p>
<p>Another promising area of research involves glycomimetics—synthetic molecules designed to mimic the structure and function of natural glycans. These compounds hold potential as therapeutic agents by modulating glycan-mediated processes, such as inflammation, infection, and cancer progression.</p>
<p><strong>Conclusion</strong></p>
<p>Glycoprotein synthesis is an intricate and tightly regulated process with profound implications for biological function and biotechnology applications. The two main pathways, N-linked and O-linked glycosylation, each contribute to the diversity and functionality of glycoproteins in distinct ways. Advances in recombinant production and glycoengineering have opened new avenues for developing therapeutic proteins with enhanced efficacy.</p>
<p>As the field of glycoprotein research continues to evolve, the ability to manipulate glycan structures will unlock new opportunities in diagnostics, drug development, and personalized medicine. Overcoming challenges related to glycan heterogeneity and improving analytical techniques will be critical for the next generation of biopharmaceuticals. Glycoproteins, with their multifaceted roles, will remain at the forefront of molecular biology and therapeutic innovation.</p>
<p><strong>Unlock the Potential of Custom Glycoprotein Synthesis for Your Research</strong></p>
<p>At Creative Biolabs, we understand the significance of high-quality glycoprotein synthesis in advancing your research and therapeutic developments. Our custom glycoprotein synthesis services are designed to meet diverse research needs, utilizing innovative methods to create homogeneous glycoproteins with precise glycan structures.</p>
<p>Our comprehensive services include:</p>
<ul>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-remodelling-for-glycoprotein-synthesis.htm"><strong>Glycoprotein Remodeling for Glycoprotein Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/native-chemical-ligation-for-glycoprotein-synthesis.htm"><strong>Native Chemical Ligation for Glycoprotein Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/expressed-protein-ligation-for-glycoprotein-synthesis.htm"><strong>Expressed Protein Ligation for Glycoprotein Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/staudinger-ligation-for-glycoprotein-synthesis.htm"><strong>Staudinger Ligation for Glycoprotein Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/sugar-assisted-ligation-for-glycoprotein-synthesis.htm"><strong>Sugar-assisted Ligation for Glycoprotein Synthesis</strong></a></span></li>
</ul>
<p>With a focus on delivering tailored solutions, we leverage advanced techniques and a skilled team with extensive experience in glycoprotein synthesis, capable of handling constructs of up to 150 amino acids in length. Our commitment to quality ensures that every step, from project initiation to completion, meets the highest standards in the industry.</p>
<p>Whether you are exploring new treatments or conducting fundamental research, our glycoprotein synthesis services help you overcome the complexities associated with glycan structures, providing the reliability and consistency need for impactful results. Contact us today to learn how we can support your scientific endeavors.</p>
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		<title>Recent Advances and Applications in Glycoprotein Synthesis</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/advances-applications-in-glycoprotein-synthesis/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Wed, 25 Sep 2024 10:25:30 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<category><![CDATA[Glycoprotein]]></category>
		<category><![CDATA[Glycoprotein Synthesis]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=61</guid>

					<description><![CDATA[Glycoproteins play a critical role in numerous biological processes, including cellular communication, immune regulation, and protein folding. The precise synthesis of these biomolecules is key to advancing fields like biotechnology, therapeutics, and<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/advances-applications-in-glycoprotein-synthesis/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p>Glycoproteins play a critical role in numerous biological processes, including cellular communication, immune regulation, and protein folding. The precise synthesis of these biomolecules is key to advancing fields like biotechnology, therapeutics, and diagnostics. Recent progress in <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycoprotein-synthesis.htm">glycoprotein synthesis </a></span>has centered on improving accuracy, scalability, and functionality. This blog explores new research developments, current trends, and emerging applications of glycoprotein synthesis.</p>
<p><strong>Advances in Glycoprotein Synthesis Technologies</strong></p>
<ol>
<li><strong>Cell-Free Systems for Accuracy Control</strong><br />
Cell-free synthesis is gaining popularity as it offers unparalleled control over glycan composition. Unlike traditional <em>in vivo</em> methods, cell-free systems remove the complexities associated with living cells, such as membrane barriers or cellular toxicity. These platforms allow scientists to integrate enzymes directly into the reaction environment, promoting precise glycosylation and supporting the on-demand production of specialized glycoproteins. The flexibility of these systems makes them ideal for prototyping therapeutic proteins and streamlining vaccine development efforts.</li>
<li><strong>Chemoenzymatic and Chemical Synthesis</strong><br />
<a href="https://www.creative-biolabs.com/glycoprotein/chemoenzymatic-synthesis-of-glycoproteins.htm"><span style="color: #0000ff;">Chemical synthesis</span></a>, often combined with chemoenzymatic techniques, has advanced to produce glycoproteins with homogenous glycan structures. This accuracy facilitates studies of glycan-protein interactions, which underpin many biological mechanisms. Recent developments in click chemistry and native chemical ligation have further enhanced site-specific glycosylation, allowing the synthesis of glycoproteins not naturally found in living organisms. This is particularly beneficial for studying rare or synthetic glycan-protein linkages.</li>
<li><strong>Enzymatic Remodeling of Glycans</strong><br />
Researchers are increasingly utilizing glycosyltransferases and glycosidases to remodel existing glycoproteins, customizing their glycan profiles for specific functions. This enzymatic remodeling offers new possibilities in glycoengineering, allowing scientists to enhance the performance of therapeutic proteins by adjusting glycosylation patterns to improve efficacy or reduce immunogenicity.</li>
</ol>
<p><strong>Applications of Synthetic Glycoproteins</strong></p>
<ol>
<li><strong>Therapeutic Development</strong><br />
Glycoproteins are essential components of several biopharmaceuticals, including monoclonal antibodies and erythropoietin. Advances in synthesis technologies enable the <a href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-development.htm"><span style="color: #0000ff;">production of therapeutic proteins</span></a> with optimized glycan structures, which enhance their pharmacokinetics and efficacy. For example, glycoengineered antibodies exhibit improved antibody-dependent cellular cytotoxicity (ADCC), making them more effective in cancer treatment.</li>
<li><strong>Vaccine Innovation</strong><br />
<a href="https://www.creative-biolabs.com/glycoprotein/custom-glycoprotein-synthesis.htm"><span style="color: #0000ff;">Synthetic glycoproteins</span></a> are transforming vaccine development. By mimicking the glycosylation patterns of pathogens, researchers create antigens that generate robust immune responses. Glycoproteins also play a key role in the development of conjugate vaccines, which couple bacterial polysaccharides with carrier proteins to boost immunogenicity.</li>
<li><strong>Diagnostics and Biomarker Discovery</strong><br />
Aberrant glycosylation is a hallmark of various diseases, including cancers and autoimmune disorders. Advances in glycoprotein synthesis facilitate the creation of glycan arrays, which are critical for identifying disease biomarkers and developing diagnostic assays. These synthetic glycoproteins help scientists study glycan-protein interactions, providing new insights into disease mechanisms.</li>
<li><strong>Biotechnological Tools for Research</strong><br />
Synthetic glycoproteins are invaluable in molecular biology and biotechnology. Researchers use them to study protein stability, folding, and receptor-ligand interactions. They are also employed in developing high-throughput assays for drug discovery, aiding pharmaceutical research by providing well-characterized glycoforms of target proteins.</li>
</ol>
<p><strong>Future Directions</strong></p>
<p>The future of glycoprotein synthesis is poised to be shaped by advancements in synthetic biology and computational tools. Predictive models based on artificial intelligence are being developed to design glycoproteins with specific therapeutic or diagnostic properties. Additionally, automation and microfluidic platforms are expected to enhance synthesis efficiency, making custom glycoproteins more accessible for research and clinical applications.</p>
<p>As the demand for personalized medicine grows, glycoprotein synthesis will play a crucial role in producing tailored therapeutics and diagnostics. Further research will likely focus on overcoming scalability challenges, enabling broader use of synthetic glycoproteins across industries and enhancing their impact on global health.</p>
<p><strong>Conclusion</strong></p>
<p>Recent advances in glycoprotein synthesis, including cell-free systems, chemoenzymatic approaches, and <a href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-remodelling-for-glycoprotein-synthesis.htm"><span style="color: #0000ff;">glycan remodeling</span></a>, have expanded the potential of these molecules in various fields. From therapeutic development and vaccine production to diagnostics and basic research, synthetic glycoproteins are becoming indispensable tools. As technology continues to evolve, these innovations will shape the future of medicine and biotechnology, paving the way for new discoveries and improved healthcare solutions.</p>
<p><strong>Transform Your Research with Custom Glycoprotein Synthesis</strong></p>
<p>At Creative Biolabs, we recognize the pivotal role glycoproteins play in various biological processes and therapeutic applications. Our custom <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycoprotein-synthesis.htm">glycoprotein synthesis services</a></span> are designed to facilitate your research and development needs with exceptional quality and efficiency. Utilizing advanced methodologies and a team of experienced experts, we offer a comprehensive range of services tailored to meet your specific requirements.</p>
<p>Our offerings include:</p>
<ul>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycan-synthesis.htm"><strong>Custom Glycan Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycopeptide-synthesis.htm"><strong>Custom Glycopeptide Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycoprotein-synthesis.htm"><strong>Custom Glycoprotein Synthesis</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-remodelling-for-glycoprotein-synthesis.htm"><strong>Glycoprotein Remodeling</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/native-chemical-ligation-for-glycoprotein-synthesis.htm"><strong>Native Chemical Ligation</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/expressed-protein-ligation-for-glycoprotein-synthesis.htm"><strong>Expressed Protein Ligation</strong></a></span></li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/staudinger-ligation-for-glycoprotein-synthesis.htm"><strong><span style="color: #0000ff;">Staudinger Ligation</span></strong></a></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/sugar-assisted-ligation-for-glycoprotein-synthesis.htm"><strong>Sugar-assisted Ligation</strong></a></span></li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/oligosaccharide-library-development-service.htm"><strong>Oligosaccharide Library Development</strong></a></span></li>
</ul>
<p>Our custom synthesis solutions help you overcome the complexities of glycoprotein production, whether for research or therapeutic purposes. We guarantee high-quality results while maintaining affordability, ensuring that you receive the best value for your investment. Our professionals are dedicated to offering targeted assistance throughout the synthesis process, ensuring that your project progresses smoothly and effectively.</p>
<p>If you are looking to enhance the quality and efficacy of your research, explore our custom glycoprotein synthesis services today. Get in touch with us to discuss how we can assist you in achieving your research goals.</p>
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		<item>
		<title>Therapeutic Glycoproteins: Advances in Research and Potential Applications</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/therapeutic-glycoproteins-advances-in-research-applications/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Wed, 14 Aug 2024 05:45:02 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<category><![CDATA[Glycoprotein]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=51</guid>

					<description><![CDATA[Therapeutic glycoproteins are increasingly recognized as pivotal in modern medical research, offering promising new treatments for a range of diseases. Recent advancements have provided deep insights into their structure, function, and potential<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/therapeutic-glycoproteins-advances-in-research-applications/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p><a href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-development.htm"><span style="color: #0000ff;">Therapeutic glycoproteins</span></a> are increasingly recognized as pivotal in modern medical research, offering promising new treatments for a range of diseases. Recent advancements have provided deep insights into their structure, function, and potential therapeutic applications.</p>
<p><strong>Rapid Simulation of Glycoprotein Structures</strong></p>
<p>A breakthrough in the simulation of glycoprotein structures has been achieved with the development of new software that significantly speeds up drug development processes. Researchers from the Max Planck Society introduced a method utilizing grafting and steric exclusion of glycan conformer libraries. This innovation allows for the rapid and accurate modeling of glycoprotein structures, which is essential for understanding their function and designing effective drugs.</p>
<p><strong>Monoclonal Antibodies and Viral Infections</strong></p>
<p>The development of monoclonal antibodies targeting glycoproteins has shown promising results in combating viral infections. For instance, a monoclonal antibody targeting the fusion glycoprotein of the Nipah virus—a highly lethal zoonotic pathogen—has demonstrated impressive protection in animal models and is advancing to human clinical trials. Similarly, the Inmazeb cocktail, which contains three antibodies targeting the Ebola virus glycoprotein, has proven effective in providing long-lasting immunity against various Ebolavirus species.</p>
<p><strong>Enhancing Antibody Efficacy Through Glycosylation</strong></p>
<p>A novel biotechnological approach involves manipulating polyamines to maintain antibody glycosylation profiles. This method ensures the consistent production of therapeutic proteins, such as monoclonal antibodies, by maintaining the stability of their glycan structures. This advancement has significant implications for the manufacturing and quality control of antibody drugs, potentially lowering production costs and enhancing drug efficacy.</p>
<p><strong>Therapeutic Strategies for Henipaviruses</strong></p>
<p>Understanding the structure of viral glycoproteins is essential for developing effective therapeutic strategies. A detailed study of the Henipavirus glycoprotein has identified potential targets for intervention. This research underscores the importance of the glycoprotein’s structure in designing treatments for viral infections.</p>
<p><strong>Advances in Respiratory Syncytial Virus Treatment</strong></p>
<p>Recent studies have identified a protective antibody that targets a conserved epitope on the fusion glycoprotein of the respiratory syncytial virus. This discovery opens the door to new therapeutic antibodies that can effectively neutralize Respiratory Syncytial Virus, offering the potential for improved clinical outcomes.</p>
<p><strong>New Therapies for Lassa Fever</strong></p>
<p>Studies on the Lassa virus have led to the development of a cocktail of protective antibodies capable of overcoming the virus&#8217;s dense glycan shield. This therapeutic approach offers promising treatment options for Lassa fever, a severe viral hemorrhagic illness.</p>
<p><strong>Conclusion</strong></p>
<p>Ongoing research and development in therapeutic glycoproteins are driving significant advancements in the treatment of various infectious diseases. By delving into the complex structures and functions of these glycoproteins, scientists are able to design more effective drugs and therapeutic strategies. These innovations enhance treatment efficacy and advance the broader fields of biotechnology and pharmaceuticals. As research progresses, the potential applications of therapeutic glycoproteins are expected to expand, offering new solutions for some of the world’s most challenging diseases.</p>
<p>Creative Biolabs offers a comprehensive range of glycoprotein services and products, including:</p>
<p><span style="color: #0000ff;"><strong>Glycoprotein Synthesis</strong></span></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-analysis.htm"><span style="color: #0000ff;"><strong>Glycan Structure Analysis</strong></span></a></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/therapeutic-protein-glycoengineering-service.htm"><span style="color: #0000ff;"><strong>Glycoprotein Engineering</strong></span></a></p>
<p><span style="color: #0000ff;"><strong>Glycoprotein-based Drug Development</strong></span></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/category-glycopeptide-458.htm"><span style="color: #0000ff;"><strong>Glycopeptide</strong></span></a></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/category-glycoprotein-459.htm"><span style="color: #0000ff;"><strong>Glycoprotein</strong></span></a></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/category-monosaccharides-463.htm"><span style="color: #0000ff;"><strong>Monosaccharides</strong></span></a></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/category-oligosaccharides-464.htm"><span style="color: #0000ff;"><strong>Oligosaccharides</strong></span></a></p>
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		<title>Glycoprotein Production in Mammalian Cells</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/glycoprotein-production-in-mammalian-cells/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Wed, 03 Jul 2024 05:25:49 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<category><![CDATA[Glycoprotein]]></category>
		<category><![CDATA[Mammalian Cells]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=45</guid>

					<description><![CDATA[Abstract Over the past few years, the biopharmaceutical industry has increasingly utilized mammalian cell expression systems for producing biologics. The current state of glycosylation mechanisms in these systems, along with the fact<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/glycoprotein-production-in-mammalian-cells/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<h6><span lang="EN-US">Abstract</span></h6>
<p>Over the past few years, the biopharmaceutical industry has increasingly utilized mammalian cell expression systems for producing biologics. The current state of glycosylation mechanisms in these systems, along with the fact that monoclonal antibodies are most often used as therapeutic proteins, has a big impact on how biologics develop. <a href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-development.htm"><span style="color: #0000ff;">Therapeutic recombinant glycoproteins</span></a>, including monoclonal antibodies, exhibit different biological properties due to their varied glycan profiles. Thus, developing cell genetic modification strategies not only enhances cell-specific productivity but also optimizes <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycan-profiling.htm">glycan profile</a></span> distribution to increase therapeutic activity. Moreover, advancements in &#8220;omics&#8221; technologies provide new possibilities for improving these aspects, particularly for Chinese Hamster Ovary (CHO) cells.</p>
<h4><span lang="EN-US">Cell Engineering</span></h4>
<p><strong>Expression Systems</strong></p>
<p>In the biopharmaceutical industry, glycoprotein production is achieved through either transient or stable gene expression in mammalian cells. Transient expression is preferred for rapid and cost-effective methods as it bypasses the lengthy process of integrating plasmids into the genome, making it significantly faster. However, the production rate depends on various factors, including transfection efficiency, the cytotoxicity of transfection reagents, and the long-term fed-batch culture strategy. Although the protein levels obtained are not as high as those from stable gene expression systems, transient transfection remains suitable for many applications, especially high-throughput screening and early product characterization. To date, only viral vectors for gene therapy have been produced through transient transfection and have been clinically applied.</p>
<p>When large-scale glycoprotein production is required, stable gene expression systems are the preferred method. For these systems, several aspects have been processed and optimized to enhance productivity, process robustness, and reduce cell line generation time. Stable gene expression involves integrating the gene of interest into the host cell genome, where it can be maintained and expressed over many generations of cell division.</p>
<p><strong>Selection Systems</strong></p>
<p>Over the years, numerous selection systems have been developed to enhance protein production rates and selection efficiency. For stable expression, gene markers are typically integrated into the expression plasmid along with the cDNA encoding the target gene. The number of integrated plasmid copies and the integration site in the host genome are crucial factors. Common selection markers in the biopharmaceutical industry include the glutamine synthetase (GS) and dihydrofolate reductase (DHFR) genes. TNS0 and Sp2/0 cell lines lack sufficient endogenous GS expression, allowing for selection by simply removing glutamine from the medium. For CHO cells, combining methionine sulfoximine (MSX, a glutamine analog) with glutamine-free medium inhibits endogenous GS activity, providing sufficient selection pressure. Additionally, recent developments in CHO GS-knockout (KO) cell lines have increased the stringency of the selection system.</p>
<p>Similarly, the DHFR selection system uses CHO cell lines deficient in DHFR. By integrating the recombinant DHFR gene into the plasmid and subjecting the cells to increasing concentrations of methotrexate (which inhibits DHFR enzyme activity) and nucleic acid precursor starvation, the target gene is amplified. Other selection systems, such as the Oscar<img src="https://s.w.org/images/core/emoji/14.0.0/72x72/2122.png" alt="™" class="wp-smiley" style="height: 1em; max-height: 1em;" /> system from the University of Edinburgh, utilize hypoxanthine-guanine phosphoribosyltransferase (HPRT) for purine synthesis, although DHFR and GS systems remain the most widely used for large-scale commercial production.</p>
<p><strong>Gene Expression</strong></p>
<p>Despite the success of these selection systems, they still face a major issue: they rely on random plasmid integration and expression in the host genome. This randomness produces heterogeneous cell populations with varying expression levels across clones. Transgenes may be inserted into heterochromatin regions, leading to very weak gene expression. This necessitates screening numerous clones (typically hundreds to thousands) to find those with plasmids integrated into highly active chromatin regions (&#8220;hot spots&#8221;). Recently, several molecular and cellular biology tools have been developed for targeted gene integration, reducing the randomness of gene insertion and increasing predictability for high transgene expression.</p>
<p>Recombinase-mediated cassette exchange (RMCE) and site-specific nucleases like Zinc Finger Nucleases, Transcription Activator-Like Effector Nucleases (TALEN), and CRISPR/Cas9 have shown promise in this regard. RMCE utilizes site-specific recombinases to exchange specific sequence cassettes on plasmids with corresponding sequences in the host genome. This technique improves the success rate and reduces the time required to develop stable cell lines expressing monoclonal antibodies. The second generation of tools, including TALEN, and CRISPR/Cas9, induce double-strand breaks at precise locations in the host genome, facilitating targeted integration through non-homologous end joining (NHEJ) or homologous recombination (HDR).</p>
<p><strong>Cell Growth, Proliferation, and Survival</strong></p>
<p>Optimizing cell growth, proliferation, and survival is crucial for maximizing protein yield in mammalian cell expression systems. Process parameters such as pH, temperature, and mixing, along with media formulation, play vital roles in this optimization. Commercial media formulations are often proprietary, making the optimization resource-intensive. Additionally, small molecules from chemical libraries, such as sodium butyrate (NAB) and valproic acid (VPA), can enhance protein yield by maintaining chromatin in an open configuration through histone acetylation.</p>
<p>Optimizing the timing and concentration of these inhibitors is essential to mitigating unwanted effects like cell cycle arrest or apoptosis. Combining these inhibitors with other strategies, such as reduced temperature (30–32 °C) during the production phase, can further improve productivity by slowing down cell cycle progression and shifting cells from a proliferative to a production mode. Anti-apoptotic engineering strategies, including the overexpression of Bcl-2 family genes (Bcl-2, Bcl-xL, and Mcl-1) and downregulation of pro-apoptotic genes (Bax, Bak, Caspase-3, -7, -8, and -9), have been shown to enhance cell survival and protein yield.</p>
<p><strong>Protein Folding and Secretion</strong></p>
<p>Proper folding and secretion of glycoproteins are critical for producing functional therapeutic proteins. As proteins are translated, they undergo glycosylation and folding in the endoplasmic reticulum (ER) and Golgi apparatus before secretion. The levels of ER-associated proteins and molecular chaperones significantly impact protein folding. Overexpression of certain chaperones and folding enzymes, such as protein disulfide isomerase (PDI) and BiP, has been shown to improve productivity in some cases. However, results can be mixed, depending on the host cell line and the specific protein being produced.</p>
<p>ER stress response elements like X-box binding protein 1 (XBP-1) and glucose-regulated protein 78 (GRP78) are also crucial for proper protein folding. Overexpression of XBP-1, a transcription factor involved in the unfolded protein response (UPR), has shown positive effects on protein production in some studies. Another key factor is GADD34, which restores translation by dephosphorylating eukaryotic initiation factor 2 alpha (eIF2α) under ER stress, thereby enhancing protein production levels.</p>
<p><strong>Glycosylation Optimization</strong></p>
<p><a href="https://www.creative-biolabs.com/glycoprotein/glycosylation-of-therapeutic-protein.htm"><span style="color: #0000ff;">Glycosylation</span></a> is a critical post-translational modification affecting the stability, efficacy, and immunogenicity of therapeutic glycoproteins. CHO cells, the most commonly used mammalian cell line for glycoprotein production, do not replicate all human glycosylation types, such as α-2,6-sialylation and α-1,3/4-fucosylation. Efforts in metabolic engineering and genetic modification aim to address these limitations by introducing human glycosylation pathways into CHO cells. For example, introducing enzymes like sialyltransferases and fucosyltransferases can help achieve more human-like glycosylation patterns.</p>
<h4><span lang="EN-US">Conclusion</span></h4>
<p>The production of therapeutic glycoproteins in mammalian cells has seen significant advancements, driven by the need for optimized glycosylation, enhanced cell productivity, and robust expression systems. CHO cells remain the workhorse for glycoprotein production, but ongoing research and development efforts continue to improve their efficiency and the quality of the glycoproteins they produce. Future innovations in cell engineering, process optimization, and glycosylation control will further advance the field, ensuring the availability of high-quality therapeutic proteins to meet growing healthcare demands.</p>
<p>The services and products provided by Creative Biolabs are as follows:</p>
<table style="border-collapse: collapse; width: 100%;">
<tbody>
<tr>
<td style="width: 50%;">Product Name</td>
<td style="width: 50%;">Type</td>
</tr>
<tr>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/recombinant-mouse-alpha-1-b-glycoprotein-1168.htm">Recombinant Mouse Alpha-1-b glycoprotein (A1BG) (Met22-Ser219) [His-tag and S-tag], E. coli</a> </span></td>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/category-glycoprotein-459.htm">Glycoprotein</a></span></td>
</tr>
<tr>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/mycobacterium-bovis-mpb83-48-62-tt-o-man-4642.htm">Mycobacterium bovis MPB83 (48-62): TT(O-Man-O-Man)AAMADPAADLIGR-NH<sub>2</sub></a></span></td>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/category-glycopeptide-458.htm">Glycopeptide</a></span></td>
</tr>
<tr>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/4-cyclohexyl-n-2-hydroxyethyl-glycyl-227.htm">4-Cyclohexyl-N-((2-hydroxyethyl)glycyl)butanamide</a></span></td>
<td style="width: 50%;"><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/category-carbohydrate-based-surfactant-470.htm">Carbohydrate-based Surfactant</a></span></td>
</tr>
</tbody>
</table>
<ul>
<li><span style="color: #0000ff;"><strong><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/bio-better-glucocerebrosidase-glycoengineering.htm">Bio-better Glucocerebrosidase Glycoengineering Service</a></strong></span></li>
<li><span style="color: #0000ff;"><strong><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/bio-better-glucarpidase-glycoengineering.htm">Bio-better Glucarpidase Glycoengineering Service</a></strong></span></li>
<li><strong><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoengineering-of-antibody.htm">Therapeutic Antibody Glycoengineering</a> <a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/cell-line-glycoengineering.htm">Cell Line Glycoengineering</a></span></strong></li>
</ul>
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		<title>Recent Progress in Glycobiology Microarray Research</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/recent-progress-in-glycobiology-microarray-research/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Sat, 22 Jun 2024 10:35:40 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<category><![CDATA[Glycoprotein]]></category>
		<category><![CDATA[glycoprotein microarray]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=66</guid>

					<description><![CDATA[Introduction Glycobiology microarrays are essential tools for high-throughput analysis of glycan-protein interactions. With continuous advancements, these arrays are facilitating a deeper understanding of immune responses, cancer diagnostics, drug discovery, and infectious disease<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/recent-progress-in-glycobiology-microarray-research/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p><strong>Introduction</strong><br />
<span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycobiology-microarray.htm">Glycobiology microarrays</a></span> are essential tools for high-throughput analysis of glycan-protein interactions. With continuous advancements, these arrays are facilitating a deeper understanding of immune responses, cancer diagnostics, drug discovery, and infectious disease research. This article delves into the latest research trends and innovations in glycobiology microarray technologies.</p>
<p><strong>Advances in Glycan Detection and Microarray Sensitivity</strong></p>
<p>Recent developments have improved the sensitivity of microarrays, making it possible to analyze even minor glycan variations. Researchers are adopting nanopore sequencing technologies, chemically tagging nanopores, and integrating glycan-binding proteins to enhance detection accuracy.</p>
<p><strong>Hybrid Microarrays: Merging <em>In Silico</em> and Experimental Approaches</strong></p>
<p>The use of hybrid microarrays combines computational and experimental methods. Scientists design optimized glycan structures using computational modeling before testing them experimentally. This approach accelerates the discovery of new biomarkers and therapeutic targets, especially in cancer and infectious disease research.</p>
<p><strong>Cancer Research and Glycobiology Microarrays</strong></p>
<p>Microarrays are proving instrumental in identifying tumor-associated carbohydrate antigens (TACAs). These unique glycans on cancer cell surfaces serve as targets for anticancer vaccines and novel therapies. Microarrays help map the structural intricacies of these antigens, paving the way for improved therapeutic strategies and personalized medicine.</p>
<p><strong>Nanopore Technology and Glycan Sequencing</strong></p>
<p>Nanopore technology, initially used for DNA sequencing, is now being adapted for <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycan-sequencing.htm">glycan analysis</a></span>. Researchers are developing biological and artificial nanopores with site-directed modifications to accommodate the complexity of glycans. Hybrid nanopores, which combine biological elements with solid-state technologies, promise robust and scalable sequencing capabilities, enhancing both diagnostic and research applications.</p>
<p><strong>Microarray Innovations in Infectious Disease Research</strong></p>
<p>Pathogens rely on specific glycan structures for host-cell recognition and infection. By studying microbial glycan coats through microarrays, researchers can gain insights into these interactions, aiding the development of novel antimicrobial therapies and vaccines. Such studies are essential in the fight against emerging infectious diseases.</p>
<p><strong>Conclusion</strong></p>
<p>Glycobiology microarrays are at the forefront of biomedical research, providing unprecedented insights into complex glycan interactions. Advances in nanopore technology, hybrid microarrays, and targeted applications in oncology and infectious diseases demonstrate the transformative potential of these tools. As research progresses, glycobiology microarrays will continue to enhance therapeutic discoveries and deepen the understanding of glycan biology in health and disease.</p>
<p><strong>Unlocking Glycoprotein Potential: Comprehensive Services for Your Research Needs</strong></p>
<p>At Creative Biolabs, we understand the critical role glycobiology plays in the life sciences, particularly in glycoprotein research. Our advanced <span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycobiology-microarray.htm">glycobiology microarray platform</a></span> is designed to meet the diverse needs of researchers by offering a wide range of carbohydrate types affixed to chips. This tailored approach ensures you have access to the specific tools necessary for your unique experiments.</p>
<p>The versatility of our glycobiology microarray technology allows us to support a variety of studies, from basic research to applied sciences. In addition to our microarray services, we provide a comprehensive suite of glycoprotein-related services to facilitate your research:</p>
<ul>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-synthesis.htm"><strong>Custom Synthesis</strong></a></span><strong>:</strong> We offer custom synthesis of glycoproteins tailored to your specific project needs, ensuring high quality and reliability.</li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/glycoengineering-service.htm"><strong><span style="color: #0000ff;">Glycoengineering Service</span></strong></a><strong>:</strong> Our glycoengineering capabilities allow for the modification and optimization of glycoprotein structures, enhancing their functionality for therapeutic applications.</li>
<li><span style="color: #0000ff;"><a style="color: #0000ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-analysis.htm"><strong>Glycoprotein Analysis</strong></a></span><strong>:</strong> Leverage our analytical services to characterize and quantify glycoproteins effectively, helping you understand their biological roles.</li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/anti-glycoprotein-antibody-development.htm"><strong><span style="color: #0000ff;">Anti-Glycoprotein Antibody Development</span></strong></a><strong>:</strong> We specialize in developing antibodies against glycoproteins, which are essential for various research applications and diagnostics.</li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/tumor-glyco-diag-service.htm"><strong><span style="color: #0000ff;">Tumor Glyco-diag Service</span></strong></a><strong>:</strong> Our tumor glyco-diagnostics services aid in identifying glycan biomarkers associated with different cancers, advancing the field of oncological research.</li>
</ul>
<p>By integrating these services into your research workflow, we aim to provide valuable insights and accelerate discoveries in glycobiology. Partner with us to harness the full potential of glycobiology in your work. Your success is our priority, and we are committed to supporting you every step of the way. For more detailed information about our offerings, feel free to reach out to our professional team.</p>
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		<title>[Cell Host] Production of Therapeutic Glycoproteins in Mammalian Cells</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/production-of-therapeutic-glycoproteins-mammalian/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Wed, 24 Apr 2024 05:41:05 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=38</guid>

					<description><![CDATA[Over the past few years, mammalian cell expression systems have gained attention in the biopharmaceutical industry for producing biologics. The current status of glycosylation mechanisms in these systems, coupled with the prevalence<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/production-of-therapeutic-glycoproteins-mammalian/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p>Over the past few years, mammalian cell expression systems have gained attention in the biopharmaceutical industry for producing biologics. The current status of glycosylation mechanisms in these systems, coupled with the prevalence of monoclonal antibodies as today&#8217;s predominant therapeutic proteins, has significantly shaped the trajectory of biologics development. Therapeutic recombinant glycoproteins, including monoclonal antibodies, exhibit different biological properties due to their varied <span style="color: #33cccc;"><a style="color: #33cccc;" href="https://www.creative-biolabs.com/glycoprotein/glycan-profiling.htm"><span style="color: #3366ff;">glycan profiles</span></a></span>. Therefore, the development of cell genetic modification strategies aims not only to enhance the cell-specific productivity but also to optimize glycan profile distribution to increase therapeutic activity. In addition, advancements in &#8220;omics&#8221; technologies provide new possibilities for improving the expression of these aspects, which is of great help to the development of new strategies, especially CHO cells.</p>
<p>Recent estimates value the biologics market at $140 billion, comprising over 200 therapies, with a substantial portion constituting recombinant glycoproteins, increasingly produced in cell-expressed products. This trend underscores a heightened emphasis on post-translational modifications, particularly <span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/glycosylation-of-therapeutic-protein.htm">glycosylation</a></span>, in biologics production. In fact, Extensive efforts in recent years have been directed towards understanding how glycosylation affects the therapeutic biological activity. Studies indicate that appropriate glycosylation can enhance recombinant protein properties, such as increasing the stability and prolonging blood circulation half-life, while mitigating immunogenicity.</p>
<p>Among mammalian cell expression systems, CHO cells are by far the most commonly used cell line, contributing to over 70% of recombinant biological protein production, primarily monoclonal antibodies. This review focuses on recent advancements in <span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-production-in-mammalian-cells.htm">mammalian cell glycoprotein production</a></span>, with a focus on CHO cells. We outline the various expression systems currently used for therapeutic glycoprotein production and discuss cell engineering strategies aimed at enhancing biologics production and quality optimization. Finally, we highlight recent trials employing diverse &#8220;omics&#8221; approaches to improve glycoprotein production and glycosylation.</p>
<p>Cell Host</p>
<ul>
<li>CHO Cells</li>
</ul>
<p>Because the recombinant glycoprotein produced by CHO cells has the same sugar chain as humans, the resulting product is more likely to be compatible and biologically active in human host cells. Additionally, these cells are impervious to interference from human viruses, minimizing biosafety risks for commercial production. This resilience stems from the absence of genes facilitating viral entry into CHO cells. Different gene amplification systems have been developed in CHO cells with high titers and yields. Currently, many biotherapeutic glycoproteins approved by regulatory bodies like EMA are manufactured using CHO cells. These include well-known monoclonal antibodies such as Siltuximab (SYLVANT<sup>®</sup>), Pertuzumab (PERJETA<sup>®</sup>) and Rituximab (RITUXAN<sup>®</sup>), as well as other tissue plasminogen activators (tPa, ACTILYSE®, ACTIVASE<sup>®</sup>) and human deoxyribonuclease (PULMOZYME<sup>®</sup>). In fact, more than half of the 13 new biologics approved in 2015 were recombinant glycoproteins produced in CHO cells. Notably, several monoclonal antibodies approved in recent years, such as daratumumab (DARZALEX<sup>®</sup>), and mepolizumab (NUCALA<sup>®</sup>), Evolocumab, used to treat conditions like multiple myeloma, asthma, and hypercholesterolemia, are also produced in CHO cells. Despite these advantages, CHO cells do not replicate all human glycosylation types, such as α-2,6-sialylation and α-1,3/4-fucosylation. In addition, polysaccharides produced by CHO cells do not occur in human cells, with certain structures like N-glycolylneuraminic acid (Neu5Gc) and galactose-α-1,3-galactose (α-gal) being either absent or present at very low levels. The human immune system can produce antibodies, and these structures can contribute to the neutralization of the immunogenicity of relevant biotherapeutics. While efforts in metabolic engineering have shown some progress, CHO cells still face limitations in producing certain γ-carboxylate recombinant proteins such as coagulation factors (Kumar 2015). Moreover, proteins requiring proteolysis for maturation may not undergo complete cleavage and activation in CHO cells. For example, industrial-scale co-expression of Furin in CHO cells has demonstrated fully cleaved and active von Willebrand factor and coagulation factor VIII B. Similarly, co-expression of protein precursor convertase and human osteogenic protein-7 has been achieved in CHO cells.</p>
<ul>
<li>Human Cell Lines</li>
</ul>
<p>One way to produce human-analogous glycosylation is employing human cell lines for recombinant glycoprotein production. While this strategy may not ensure the ideal glycosylation mode, it does yield non-immunogenic polysaccharides. Among the human cell lines commonly used for therapeutic glycoprotein production are HEK293 cells and HT-1080 cells, derived from human kidney and embryonic fibroma, respectively. Drotrecogin alfa (Xigris<sup>®</sup>), the first therapeutic glycoprotein produced in human cells, gained the EMA approval in 2001 and 2002. However, it was withdrawn from the market in 2011 due to insufficient beneficial therapeutic efficacy. Subsequently, four glycoproteins were approved for treatment, namely glucosidase alpha, erythropoietin (DYNEPO<sup>®</sup>), Idursulfase (ELAPRASE<sup>®</sup>) and Velaglucerase alfa (VPRIV<sup>®</sup>), all produced in HT-1080 cells using gene activation techniques. Notably, Epoeitin delta, produced by HT-1080 cells, exhibited superior homogeneity of tetra-antennary glycans, higher sialic acid, and no tetra-antennary glycans compared to its CHO cell counterpart. However, commercial reasons led to its withdrawal from the market. Velaglucerase alfa displayed a glycan profile akin to products from in other CHO and carrot cells of the same species (CEREZYME<sup>®</sup> and ELELYSO<sup>®</sup>). Despite differing glycan profiles, these products demonstrated similar <em>in vitro</em> enzymatic activity, stability, and efficacy, although 24% of patients developed neutralizing anti-imiglucerase antibodies impacting protein activity.</p>
<p>In 2014, a large number of therapeutic proteins produced in human cell lines were approved, including four new glycoproteins approved by the EMA. rFVIIIFc (ALPROLIX<sup>®</sup>) and rFIXFc (ELOCTATE<sup>®</sup>) stand out, designed to mitigate bleeding in patients afflicted with hemophilia A and B. They include FVIII and FIX protein domains fused to the Fc portion of IgG1. rFVIIIFc has six tyrosine sulfation positions vital for its functionality, while the carboxylation of the first dodeca-carboxyglutamic acid residue in rFIXFc is pivotal for its activity. Expression of these glycoproteins in HEK293 cells provides better tyrosine sulfation compared to CHO cells, with the added advantage of producing the product without any α-gal and Neu5Gc. Another noteworthy mention is TRULICITY<sup>®</sup>, a Fc fusion protein approved in 2014 for type 2 diabetes treatment, manufactured by HEK293-EBNA1 cells. Human-clrhFVIII (NUWIQ<sup>®</sup>), serving as a clotting factor replacement for disabled hemophilia A, garnered approval from the EMA in 2014, respectively. It is synthesized in the HEK293-F cell line, exhibiting a protein profile akin to factor VIII but without α-gal and Neu5Gc.</p>
<p>Currently, various human cell lines are under utilization for recombinant glycoprotein production, undergoing pre-clinical or clinical development phases. PER.C6 cells, containing transformed type 5 E1A and E1B-encoding sequences derived from human embryogenic retinal cells, demonstrate the capability to yield high titers of IgG without the necessity for gene amplification. MOR103, a colony-stimulating factor of monoclonal antibodies targeting granulocyte-macrophages, is being developed to treat rheumatoid arthritis and multiple sclerosis. CL184, a monoclonal antibody used for rabies virus, is undergoing clinical trials phase 1/2 after being produced by PER.C6 cells. The HKB-11 cell line, a fusion of HEK293S and the human B cell line, recently exhibited elevated levels of protein production with α-2,3 and α-2, 6-sialic acid conjugates. Additionally, human amniotic fluid cells and CAP (CEVEC&#8217;s Amniocyte Production) cells originating from human liver cancer HuH-7 cells are currently undergoing preclinical evaluation, demonstrating promising results akin to human glycosylation patterns.</p>
<ul>
<li>Other Mammalian Cell Lines (Non-human)</li>
</ul>
<p>Baby hamster kidney (BHK) cells are mainly used for vaccine production, with only two recombinant proteins currently produced using these cells. Notably, clotting factors such as Factor VIIa (NovoSeven<sup>®</sup>) and Factor VIII (Kogenate<sup>®</sup> and Kovaltry<sup>®</sup>) are among them. These large glycoproteins, rich in sugar groups and disulfide bonds pose significant challenges during production.</p>
<p>Mouse myeloma cells (NS0 and Sp2/0), generated from tumor cells, are not used to produce endogenous immunoglobulins but are harnessed for monoclonal antibody production. Examples include cetuximab (ERBITUX<sup>®</sup>) and Palivir Co., Ltd. (SYNAGIS<sup>®</sup>).</p>
<ul>
<li>Non-Mammalian Cell Lines and Other Expression Systems</li>
</ul>
<p>In the past decade, a notable trend has been the increasing use of mammalian cells for producing recombinant glycoproteins. However, it&#8217;s essential to remember that a substantial number of recombinant proteins continue to be generated using other expression systems. These systems lack sufficient glycosylation capacity due to the absence of requisite enzymes, thereby mainly facilitating non-glycosylated expression. Bacterial expression systems boast rapid growth and high yields, yet encounter protein accumulation as there&#8217;s no accompanying mechanism for extracting proteins from inclusion bodies before <em>in vitro</em> replication. Notably, commercially available unglycosylated enzymes like asparaginase and collagenase are produced in bacterial expression systems. Yeast expression systems, known for their rapid division and high yields, are also utilized. Therapeutic proteins produced via yeast expression systems include ocriplasmin (JETREA<sup>®</sup>) and catridecagog (TRETTEN<sup>®</sup>). Insect and plant cells have the capability to produce recombinant proteins with complex sugar chain structures, albeit different from those found in humans. Plant cell production involves alpha-1, 3-fructose and β-1, 2-xylose, absent in human cells, thereby potentially triggering immune responses. Insect cells undergo modification to yield high-mannose or oligomannose structures before N-glycochain production. Notably, glycoproteins produced in plant and insect cells lack sugar chains on sialic acid residues. Notable treatments produced via insect cell expression systems are the human papillomavirus vaccine (CERVARIX<sup>®</sup>), prostate cancer immunotherapy (PROVENGE<sup>®</sup>), and influenza vaccine (FLUBLOK<sup>®</sup>). Additionally, some therapeutic proteins are produced in transgenic animals, which, like other mammalian cell expression systems, often exhibit glycosylation patterns differing from native human proteins. Notable examples include the production of human antithrombin from genetically modified goats as the first therapeutic drug on the market utilizing genetically modified animals. The C1-esterase inhibitor (Ruconest®) produced from rabbit milk, gained approval from the EMA in 2011. The third product is a genetically modified egg produced with recombinant human lysosomal acidifying lipase approved by the EMA in 2015.</p>
<p>The services and products provided by Creative Biolabs are as follows:</p>
<table style="border-collapse: collapse; width: 100%;">
<tbody>
<tr>
<td style="width: 50%;">Product Name</td>
<td style="width: 50%;">Type</td>
</tr>
<tr>
<td style="width: 50%;"><span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/tetraglucoside-cas-35175-16-7-640.htm">Tetraglucoside (CAT#: GOS0205S)</a></span></td>
<td style="width: 50%;"><span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/category-oligosaccharides-464.htm">Oligosaccharides</a></span></td>
</tr>
<tr>
<td style="width: 50%;"><a href="https://www.creative-biolabs.com/glycoprotein/sodium-mannuronate-cas-921-56-2-1018.htm"><span style="color: #3366ff;">Sodium mannuronate (CAT#: GMS0389S)</span></a></td>
<td style="width: 50%;"><a href="https://www.creative-biolabs.com/glycoprotein/category-monosaccharides-463.htm"><span style="color: #3366ff;">Monosaccharides</span></a></td>
</tr>
<tr>
<td style="width: 50%;"><a href="https://www.creative-biolabs.com/glycoprotein/rhamnolipid-1136.htm"><span style="color: #3366ff;">Rhamnolipid (CAT#: GCS0115S)</span></a></td>
<td style="width: 50%;"><span style="color: #3366ff;">Carbohydrate-based surfactants</span></td>
</tr>
</tbody>
</table>
<ul>
<li><span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoprotein-production-system.htm">Glyco-engineered Systems for Therapeutic Glycoprotein Development</a></span></li>
<li><span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/glycoengineering-service.htm">Glycoengineering Services</a></span></li>
<li><span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/custom-glycan-synthesis.htm">Custom Glycan Synthesis</a></span></li>
</ul>
<p>&nbsp;</p>
<p>Reference: Marie-Eve Lalonde., <em>et al.</em> “Therapeutic glycoprotein production in mammalian cells.” <em>Journal of biotechnology.</em> 2017, 251: 128-140.</p>
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		<title>Effects of N-glycosylation on therapeutic protein stability, pharmacokinetics, and immunogenicity</title>
		<link>https://www.creative-biolabs.com/blog/glycoprotein/therapeutic-protein-stability/</link>
		
		<dc:creator><![CDATA[biolabs]]></dc:creator>
		<pubDate>Thu, 25 Jan 2024 01:52:47 +0000</pubDate>
				<category><![CDATA[Therapeutic Glycoprotein Research]]></category>
		<guid isPermaLink="false">https://www.creative-biolabs.com/blog/glycoprotein/?p=1</guid>

					<description><![CDATA[N-glycosylation is one of the major post-translational modifications in nature, and its influence on protein structure and function is very important. N-glycosylation is mainly produced by the co-translational process of the endoplasmic<a class="moretag" href="https://www.creative-biolabs.com/blog/glycoprotein/therapeutic-protein-stability/">Read More...</a>]]></description>
										<content:encoded><![CDATA[<p>N-glycosylation is one of the major post-translational modifications in nature, and its influence on protein structure and function is very important. N-glycosylation is mainly produced by the co-translational process of the endoplasmic reticulum and is modified by a variety of glycosylases and glycosyltransferases located in the endoplasmic reticulum and Golgi apparatus. Figure 1 shows the biosynthetic process of antibody N-glycosylation. A single N-linked glycan can be connected to N297 in the CH2 domain of each heavy chain. It has a complex dual-antenna structure, in which two arms are composed of three cores. The α1,3 and α1,6 mannose linkages of mannose, such as G0F and G1F, can be extended by the addition of galactose and sialic acid, while the oligomannose 9 structure consists of a 14-saccharide N-glycan precursor in the oligosaccharide Under the action of transferase, it is transferred to the amide nitrogen of the N side chain of the nascent polypeptide, and then is sequentially trimmed by α-glucosidase to form, and the α1,2-linked mannose in Man9 is removed by α-mannosidase I. Glycans can be converted into mannooligosaccharides 5.</p>
<p><img decoding="async" fetchpriority="high" class="aligncenter size-full wp-image-27" src="http://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-1.jpg" alt="" width="889" height="355" srcset="https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-1.jpg 889w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-1-300x120.jpg 300w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-1-768x307.jpg 768w" sizes="(max-width: 889px) 100vw, 889px" /></p>
<p>Figure 2 shows the main glycan forms present in recombinant therapeutic antibodies. N-glycans, as the hydrophilic part of glycoproteins, play an important role in protein stability. They protect proteins from proteolysis by maintaining optimal conformation. The effects of aggregation and thermal denaturation. There is also a large amount of data indicating that N-glycans also play an important role in the pharmacodynamics and pharmacokinetics of recombinant <span style="color: #3366ff;"><a style="color: #3366ff;" href="https://www.creative-biolabs.com/glycoprotein/therapeutic-glycoprotein-development.htm">therapeutic  glycoproteins</a></span> and antibodies. In addition, N-glycans can also interact with a variety of Glycan-binding protein interactions promote or reduce adverse immune responses to proteins. This article mainly summarizes the impact of N-glycans on protein stability, pharmacokinetics and immunogenicity, providing a reference for optimizing N-glycosylation.</p>
<p><img decoding="async" class="aligncenter size-full wp-image-28" src="http://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-2.jpg" alt="" width="662" height="493" srcset="https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-2.jpg 662w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-2-300x223.jpg 300w" sizes="(max-width: 662px) 100vw, 662px" /></p>
<h6>Effect of N-glycosylation on protein stability</h6>
<p>N-glycans, as structural components, affect the physical and chemical properties of proteins. Chemical instability involves the formation and destruction of covalent bonds within the protein, such as deamination, oxidation, and peptide bond hydrolysis. Physical instability includes aggregation. and thermal denaturation, etc. These instabilities will lead to accelerated protein degradation or aggregation during drug storage or during patient treatment, reducing drug safety.</p>
<p>(1) Effect of N-glycosylation on the stability of recombinant cytokines and enzymes, such as erythropoietin, interferon-b, interferon-g, ribonuclease, α-galactosidase and tripeptidyl peptide Enzymes, deglycosylation of such substances will lead to increased sensitivity to thermal denaturation and proteolytic hydrolysis. For example, non-glycosylated erythropoietin lacks biological activity in vivo and shows low thermal stability.</p>
<p>(2) The effect of N-glycosylation on antibody stability. In one study, the antibody IgG1-Fc was sequentially deglycosylated with several exoglycosidases, including sialidase, β-galactosidase, β-hexosaminidase and α-mannosidase to generate proteins with different glycoforms. The results showed that the terminal galactose residue has minimal impact on the thermal stability of IgG1-Fc and the thermal stability of the CH2 domain after deglycosylation. The transition temperature is about 5℃-8℃ lower than that of glycosylated antibodies, and has lower thermal stability, proteolysis and aggregation rate.</p>
<p>(3) Glycosylation plays an important role in proteolytic stability. Deglycosylated antibodies show high susceptibility to 3 proteases (human neutrophil elastase, papain, and pepsin). Full galactose Kylation and sialylation increase the sensitivity of antibodies to papain digestion.</p>
<p>(4) Large conformational changes can occur in the polypeptide ring. The C&#8217;E ring contains N-glycosylation sites. After glycosylation, the CH2 domain will be mutated, resulting in a &#8220;closed&#8221; conformation. Since the glycan is located in the protein near the hydrophobic portion of the backbone, so removal of the N297 glycan results in strong hydrophobic interactions with the CH2 domain (Figure 3).</p>
<p><img decoding="async" class="aligncenter size-full wp-image-29" src="http://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-3.jpg" alt="" width="929" height="290" srcset="https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-3.jpg 929w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-3-300x94.jpg 300w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-3-768x240.jpg 768w" sizes="(max-width: 929px) 100vw, 929px" /></p>
<h6>Effect of N-glycosylation on protein pharmacokinetics</h6>
<p>Pharmacokinetics are directly related to the clinical effects of therapeutic proteins, with rapid clearance from serum leading to significantly increased degradation in the liver and limiting the amount of protein drugs reaching target cells. N-glycans play an important role in regulating serum concentrations of recombinant proteins, a role that is often variable and depends on the expression system or cell culture conditions.</p>
<p>(1) Sialyl glycans have a significant impact on the isoelectric point properties of glycoproteins. Therapeutic proteins containing a higher percentage of sialylated proteins contain a large number of carboxyl groups, so they have a lower isoelectric point. Since they cannot be combined with asialyl Glycoprotein receptor (ASGPR) binding and therefore exhibits a long serum half-life. Human ASGPR is composed of two type II transmembrane glycoprotein subunits, called asialoglycoprotein receptor-1 (Asgr-1) and Asgr-2. The two subunits act as hetero-oligomers or homo-oligomers. Existing in polymeric form, such as heterotrimeric form (Fig. 4a), each subunit contains a C-type carbohydrate recognition domain (CRD) and a stem region, which serves as the C-terminal extracellular domain and also contains a transmembrane region and the N-terminal cytoplasmic domain of endocytosis signaling. This protein receptor is mainly expressed on the surface of hepatocytes, binds to terminal galactose or N-acetylgalactosamine, and has a higher affinity for sugars with highly branched structures, such as three-antennary or four-antennary glycans. Physiological findings indicate that Asgr-1 is important for maintaining normal circulating levels of coagulation factor VIII (FVIII) in plasma, suggesting a role in regulating blood coagulation and thrombosis.</p>
<p>(2) ManR also has the same role. ManR (CD-206, Mrc1) is a 175kDa type I transmembrane glycoprotein, an R type CRD containing N-terminal cysteine, and then a fibronectin type II domain and 8 C type CRD as an extracellular domain, followed by a transmembrane domain and a C-terminal cytoplasmic tail (Fig. 4b). ManR can interact with proteins containing oligomannose or hybrid glycans, and then absorb therapeutic proteins from serum into intracellular lysosomes through receptor-mediated endocytosis, where they are excreted in various proteases and glycosides. Degraded by enzymes. In mouse experiments with antibodies containing oligomannose or fucosylated mannose, the researchers confirmed that human serum containing oligomannose antibodies had a shorter half-life.</p>
<p>(3) The impact of N297 glycan on antibody PK. Although deglycosylated IgG has lower stability as mentioned above, removal of glycosylation through enzymatic deglycosylation or mutagenic sugar chains has a negative impact on the antibody. There is little effect on pharmacokinetics. However, a recent study showed that a novel 2-nonglycosylated N297G mutant had a relatively high clearance rate, so this result remains to be studied.</p>
<p><img decoding="async" loading="lazy" class="aligncenter size-full wp-image-30" src="http://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-4.jpg" alt="" width="988" height="522" srcset="https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-4.jpg 988w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-4-300x159.jpg 300w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-4-768x406.jpg 768w" sizes="(max-width: 988px) 100vw, 988px" /></p>
<h6>Effect of N-glycosylation on protein immunogenicity</h6>
<p>In addition to pharmacokinetics and stability, immunogenicity is another important property related to efficiency and safety. Immunogenicity can lead to adverse clinical reactions to therapeutic proteins, such as allergic reactions and reduced efficacy. There are many factors that affect immunogenicity, including protein sequence variation, glycosylation, denervation, and aggregation. (1) Recombinant proteins with non-human glycans are immunogenic and may be pre-recognized by the immune system. Such glycans include α1,3-linked galactose (α-Gal), N-glycolyl neuron amino acid (Neu5Gc), β1,2-linked xylose, and α1,3-linked fucose, which are commonly found in recombinant glycoproteins expressed from non-human cells or other non-mammalian species. Adverse clinical immune responses to cetuximab have been reported to be related to the antibody N-glycan terminal α-Gal produced in mouse myeloma cell lines.</p>
<p>(2) In addition to non-human glycans, human N-glycans in recombinant proteins may contribute to immune regulation. Many glycan-binding proteins exist on human immune cells, especially cells of the innate immune system, including diatom proteins, galectins, and C-type lectin-like receptors (CLR or CTLR). CLRs containing C-type lectin-like domains are located on antigen-presenting cells of dendritic cells and can specifically bind to glycans such as oligomannose and fucosylated complex glycans (Table 1) to enhance T cells. tolerance.</p>
<p><img decoding="async" loading="lazy" class="aligncenter size-full wp-image-31" src="http://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-5.jpg" alt="" width="1035" height="370" srcset="https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-5.jpg 1035w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-5-300x107.jpg 300w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-5-1024x366.jpg 1024w, https://www.creative-biolabs.com/blog/glycoprotein/wp-content/uploads/sites/11/2024/01/202403-5-768x275.jpg 768w" sizes="(max-width: 1035px) 100vw, 1035px" /></p>
<p>(3) Studies have shown that enhanced tolerance needs to be mediated through the mannose 6-phosphate receptor (MPR), but only 1-3, 5 and 1-3 of the cation-independent mannose 6-phosphate receptor (CI-MPR) Only position 9 can bind to the mannose containing glycoprotein to bind to the 6-phosphate receptor surface (Figure 4c).</p>
<p>Summary: The presence of N-glycans increases the hydrophilicity of the protein and protects amino acid residues that are prone to aggregation, thereby enhancing the stability of the protein. Based on the fact that N-glycans can also affect serum half-life and immune response, during the research and development process, various therapeutic proteins should be extensively studied and optimized to improve their safety.</p>
<p>Support of Creative Biolabs</p>
<p>Creative Biolabs is a leading customer service provider in the field of therapeutic glycoprotein development. Here is a simple list of our custom services.</p>
<ul>
<li><a href="https://www.creative-biolabs.com/glycoprotein/matrix-assisted-laser-desorption-ionization-time-of-flight-mass-spectrometry-maldi-tofms.htm">MALDI-TOF MS</a></li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/high-performance-anion-exchange-chromatography-with-pulsed-amperometric-detection-hpaec-pad.htm">HPAEC-PAD</a></li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/cell-line-glycoengineering.htm">Cell Line Glycoengineering Services</a></li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/strategies-of-genetic-glycoengineering.htm">Strategies of Genetic Glycoengineering</a></li>
<li><a href="https://www.creative-biolabs.com/glycoprotein/glycan-profiling.htm">Glycan Profiling</a></li>
</ul>
<p>&nbsp;</p>
<p>Reference: QunZhou., <em>et al.</em> “The Mechanistic Impact of N-Glycosylation on Stability,Pharmacokinetics, andImmunogenicity of Therapeutic Proteins.”<em>Journal of PharmaceuticalSciences</em>.. 2023;8(3):199-221.</p>
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