Understanding the binding interactions between therapeutic candidates and various biological targets is essential for optimizing efficacy, safety, and pharmacokinetics. At Creative Biolabs, we specialize in providing high-quality binding assay services that are critical for the development and characterization of therapeutic antibodies and proteins. Our extensive array of binding assays, including Fc receptor (FcR), neonatal Fc receptor (FcRn), and complement C1q binding assays, deliver accurate, reliable, and reproducible results. Utilizing state-of-the-art technologies and unmatched expertise, Creative Biolabs delivers comprehensive solutions to meet your research and development needs.

FcR Binding Assay

The FcR binding assay is crucial for understanding how therapeutic antibodies interact with the immune system. FcγRs are found on the surface of immune cells and play a crucial role in antibody-mediated effector functions such as antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cell-mediated phagocytosis (ADCP). Our FcR binding assay encompasses a broad range of Fc receptors, such as FcγRI (CD64), FcγRIIa (CD32a), FcγRIIb (CD32b), FcγRIIIa (CD16a), and FcγRIIIb (CD16b). Using advanced platforms such as surface plasmon resonance (SPR) and flow cytometry, we assess binding kinetics and affinity with high precision.

Fig.1 Types of FcRs.^1,3

FcRn Binding Assay

FcRn is responsible for protecting IgG antibodies from lysosomal degradation, thereby extending their half-life in the circulatory system. Creative Biolabs provides precise FcRn binding assays to accurately measure the binding affinity of therapeutic antibodies under physiological conditions. Our FcRn binding assay services are meticulously designed to evaluate the binding characteristics of IgG antibodies to FcRn under both acidic and neutral pH conditions. By leveraging our expertise, we help you optimize your therapeutic candidates for better pharmacokinetics and biodistribution.

Fig.2 FcRn-mediated recycling and transcytosis.^2,3

Complement C1q Binding Assay

The complement system, especially the first component C1q, is integral to initiating the classical pathway of complement activation, which leads to the elimination of pathogens and altered cells. Our Complement C1q Binding Assay allows for the detailed evaluation of these interactions, offering insights into the antibody's potential to induce complement-dependent cytotoxicity (CDC). Employing techniques like ELISA and SPR, our assays deliver comprehensive data on C1q binding.

Our Technologies and Methods

At Creative Biolabs, we utilize cutting-edge platforms such as SPR, ELISA, and flow cytometry to ensure the highest accuracy and reliability in our binding assays. Choosing the best method for binding assays depends on the specific requirements of your study. By selecting the appropriate method, Creative Biolabs ensures that you receive the most relevant and accurate data for your therapeutic antibody and protein development projects.

• SPR and BLI are often considered the gold standards due to their ability to provide real-time kinetic data and high sensitivity.
• Flow Cytometry-based assays offer high-throughput capabilities and are particularly effective for cellular binding studies.
• ELISA, with its high specificity and sensitivity, is particularly useful for quantifying protein-protein interactions.

Advantages

• High Sensitivity and Specificity: Ensuring accurate detection of binding interactions with minimal background noise.
• Real-Time Monitoring: Providing dynamic insights into binding kinetics.
• High Throughput: Enabling the analysis of multiple samples simultaneously for efficient data generation.
• Quantitative and Qualitative Data: Offering comprehensive insights into binding affinities and mechanisms.

References

1. Ben Mkaddem, Sanae, Marc Benhamou, and Renato C. Monteiro. "Understanding Fc receptor involvement in inflammatory diseases: from mechanisms to new therapeutic tools." Frontiers in Immunology 10 (2019): 811.
2. Sand, Kine Marita Knudsen, et al. "Unraveling the interaction between FcRn and albumin: opportunities for design of albumin-based therapeutics." Frontiers in Immunology 5 (2015): 682.
3. Distributed under Open Access license CC BY 4.0, without modification.

For Research Use Only | Not For Clinical Use