Glycosylation-Specific Antibody Introduction

Glycosylation is a structurally diverse and complex protein post translational modification (PTM). Glycosylation modifications result in proteins being tagged differently, changing the conformation of peptides, and increasing protein stability. In biological research, glycosylation plays an important role. Based on our excellent hybridoma platform and phage display platform, Creative Biolabs provides comprehensive services to support the development of glycosylation-specific antibodies.

Glycosylation Modification

Glycosylation is the enzymatic process of linking sugars to proteins, lipids, and other sugars. This major PTM occurs in the endoplasmic reticulum and Golgi apparatus of all cells. The main process of glycosylation is the transfer of glycan chains to proteins by the action of glycosyltransferases, forming glycosidic bonds with amino acid residues on proteins, and completing the assembly of glycosylated proteins through a series of translocations, trimming of glycan chain ends, modifications, and fucosylation or sialylation acidification. Glycosylation is the basis of various biological processes, and small changes in glycan structure seriously affect cell biology and contribute to the onset and development of pathophysiology.

Glycosylation modifications are generally classified into five categories based on the type of modified amino acids and the properties of the glycan chains. They are N-linked glycosylation, O-linked glycosylation, phosphoserine glycosylation, C-mannosylation, and glypiation (GPI).

N-glycosylation occurs on the asparagine (Asn) residue of the peptide chain and is the most common type of glycosylation modification. It has two distinctive features: site-specificity and a pentasaccharide core. These two features provide an important basis for the analysis of N-glycoproteins/glycopeptides.

O-glycosylation usually occurs at the serine/threonine (Ser/Thr) residues of the peptide chain, where the glycan chain and the Ser/Thr side chain hydroxyl group are enzymatically catalyzed to form an O-glycosidic bond.

Phosphoserine glycosylation involves the attachment of sugars to a protein through a phosphodiester bond.

C-mannosylation is a post-translational modification of proteins in the endoplasmic reticulum. Monomeric α-mannose is attached to specific tryptophan (Trp) residues at the first Trp in the Trp-x-x-Trp/Cys (W-x-x-W/C) motif of substrate proteins by the action of C-mannosyltransferases, DPY19-related gene products.

Glycosylation is the addition of glycosylphosphatidylinositol (GPI) anchors via covalent bonds, enabling the protein to localize to the cell membrane.

Glycosylation-Specific Antibody

Glycosylation modifications are capable of regulating processes such as cell adhesion, cell ligand binding, and receptor dimerization. This allows them to participate in various physiological processes, including intracellular and extracellular signaling interactions, endocytosis, and bacterial-host recognition interactions. Also, since glycosylation is the basis of various biological processes, even small changes in glycan structure can significantly affect cell biology and contribute to the development and progression of pathophysiology, such as cancer. Malignant transformation is associated with abnormal glycosylation, and certain abnormal glycosylation patterns become cancer biomarkers. Given the regulatory role of glycosylation modifications in physiological and pathological processes, it is crucial to study them in depth. However, similar to all PTM-specific antibodies, the development of glycosylated antibodies is not an easy task.

Creative Biolabs has a wealth of knowledge about PTM specific antibody discovery. We would be delighted to share our knowledge and experience in the development of glycosylation-specific antibodies with you.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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