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Enzyme Activity Measurement of Endo-Alpha-N-Acetylgalactosaminidase

Creative Enzymes is a leader in the field of enzyme services. We have showed excellent quality with various enzyme activity services at unbeatable prices. The outstanding cost-performance ratio stays at the top of the industry. Our other advantages include the extensive experiences, cutting-edge instrument, standardized operations, and accurate analysis. We are specialized in hydrolase activity testing, including endo-alpha-N-acetylgalactosaminidase.

Endo-α-N-acetylgalactosaminidase (endo-α-GalNAcase, EC 3.2.1.97) catalyzes the hydrolysis of an O-glycosidic α linkage between galactosyl β1,3 N-acetyl-D-galactosamine (Galβ1,3GalNAc) and the serine or threonine residue in mucins andmucin-type glycoproteins from various animal sources. This O-linked disaccharide (Core 1 type O-glycan) is one of the most abundant core structures found in mucin glycoproteins. It is known as the Thomsen- Friedenreich antigen (T antigen) immunodeterminant group and is used as a specific marker of carcinoma. Endo-α-GalNAcases have been purified from Clostridium perfringens, Streptococcus pneumoniae, Alcaligenes sp., Bacillus sp., and Bifidobacterium longum. Several years ago, an endo-a-N-acetylgalactosaminidase from Bifidobacterium longum was cloned and classified into glycoside hydrolase (GH) family 101, a group newly established through the finding of this enzyme. The enzyme has a very narrow substrate specificity and could only act on the core 1 structure of O-glycans. An enzyme isolated from Streptomyces sp. has been reported to be able to release various O-glycans from O-glycoproteins such as mucin and fetuin. These endo-α-GalNAcases liberate O-linked oligosaccharides from glycoproteins without damaging the protein backbone, which makes these enzymes powerful tools for the investigation of the structure and function of O-glycans. Endo-α-GalNAcase also has applications in analysis. For example, it is ideally suited to explore the distribution and function of mucin-type glycoproteins on normal and cancer cell surfaces. Subsequently, the promising properties and functions of the enzyme has attracted many researchers to develop and commercialize new applications and products. Creative Enzymes is glad to offer activity measurement of endo-α-N-acetyl galactosaminidase to facilitate such efforts. The enzyme activity is measured using a UV spectrophotometric assay, by monitoring the release of the products.

The crystal structure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum Figure: The crystal structure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF).
Reference: Suzuki, R. et al. J. Biochem. 2009 146(3)389–398.

Creative Enzymes is fully prepared to provide accurate activity assays for endo-α-N-acetylgalactosaminidase. Possessing the superb technology, professional knowledge, and advanced equipment, Creative Enzymes always provide the top-ranked technical support and personalized customer services to satisfy any research purpose.



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