See how pretreatment with a mucin-selective protease, Mucinase StcE, for tryptic-digest sample preparation of mucins may increase the number of glycopeptides and glycoforms identified from your samples.
The basic structure of peptidoglycan (PGN) contains a carbohydrate backbone of alternating units of N-acetylglucosamine (GlcNAc) and Nacetylmuramic acid, with the N-acetylmuramic acid residues cross-linked to peptides.
Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some
Information about Glycoprotein deglycosylation. The diversity of oligosaccharide structures, both O-linked and N-linked, often results in heterogeneity in the mass and charge of glycoproteins.
Explore the structure, function, and diverse applications of Lipopolysaccharides. Discover their role in bacteria, serological specificity, and research potential.
Explore our complex carbohydrate proteins, enzyme products and kits for investigating oligosaccharides, polysaccharides, and numerous additional aspects of your carbohydrate workflow.
There are five identified glycosaminoglycan chains (see Figure 1): Hyaluronan is not sulfated, but the other glycosaminoglycan chains contain sulfate substituents at various positions of the chain.
O-Linked glycans are usually attached to the peptide chain through serine or threonine residues. O-Linked glycosylation is a true post-translational event and does not require a consensus sequence. The most common type of O-linked glycans contain an initial GalNAc residue
Learn about O-linked glycan strategies, such as the actions of O-glycosidase, how to remove di and trisialylation sialic acid residues, β-linked galactose, and N-acetylglucosamine, as well as other O-glycan modifications.
Find the right lectin for your research with our lectin selection guide, organized by lectin source/species, carbohydrate specificity, blood group specificity, and more.
Explore various strategies for deglycosylating N-linked glycans involving PNGase F, PNGase A (Glycopeptidase A), and even native and sequential deglycosylation with endoglycosidases like Endoglycosidase H, Endoglycosidase F, and exoglycosidases.
Protein Deglycosylation: PNGase F Proteomics Grade, Native Protein Deglycosylation Kit, Enzymatic Protein Deglycosylation Kit, and ProteoProfile Trypsin In-Gel Digest Kit
O-Linked glycoproteins are usually large proteins with a molecular mass of >200 kDa. Glycosylation generally occurs in high-density clusters and may represent as much as 50-80% of the overall mass.
Glycoprofile Labeling Kits for Glycan Analysis designed for efficient labeling of N-linked, O-linked and glycosylphosphatidylinositol (GPI) anchored glycans using your choice of 2-aminobenzamide (2-AB) or 2-aminobenzoic acid (anthranilic acid; 2-AA) 1,2
Structural modifications of proteins are essential to living cells. When aberrantly regulated they are often the basis of disease. Glycans are responsible for much of the structural variation in biologic systems, and their representation on cell surfaces is commonly called