Glycobiology profiling is critical to many areas of research. For example, glycosylation is one of the most common and impactful modifications found in biologic systems. It is seen in the simplest of prokaryotes and the most complex multicellular organisms, attached to proteins, lipids, and even RNA playing roles in structure, function, and regulation. As the knowledge base and methods evolve, scientists need the right tools for the job. We are filling your toolbox with glycobiology reagents and tools like enzymes, resins, labels, and reagents to aid in the discovery and experimentation around glycobiology.
To accommodate your glycobiology workflow needs, we offer a wide range of products for functional and structural analysis of glycans, including glycoprocessing and glycosylation enzymes, glycan labels, lectins, capture resins, standards, glycoproteins, and free oligosaccharides. This includes offerings of carbohydrate-recognizing proteins such as lectins and galectins, carbohydrate-active enzymes like glycosidases (exoglycosidases, endoglycosidases), and glycosyltransferases. Additionally, our GlycoProfile™ kits are a curated product line that have been developed to simplify common workflows including release and labeling of N-linked and O-linked glycans.
The glycobiology profiling tools we offer can be broken into these 4 categories:
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.
Find the right lectin for your research with our lectin selection guide, organized by lectin source/species, carbohydrate specificity, blood group specificity, and more.
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.
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 nucleoside mono- or diphosphate sugar donors.
Hyaluronan is a major component of the extracellular matrix. It’s the simplest glycosaminoglycan, and it plays several biological roles.
Review article and products for sialic acid synthesis and signaling.
Explore our complex carbohydrate proteins, enzyme products and kits for investigating oligosaccharides, polysaccharides, and numerous additional aspects of your carbohydrate workflow.
The presence of multiple functional groups and stereocenters in complex carbohydrates makes them challenging targets for the organic chemist.
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.
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.
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 the “glycome.”
The development of modern mass spectrometry (MS) equipment with high resolution and mass accuracy has led to its use in analyzing glycans for both profiling and structural studies.
HPLC Analysis of Glycans
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