|Other Names||Beta-1, 4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III, GNT-III, GlcNAc-T III, N-acetylglucosaminyltransferase III, MGAT3, GGNT3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2411a was selected from the N-term region of human MGAT3 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. MGAT3 (N-acetylglucosaminyltransferase III) transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Expression of this gene may be controlled by a multiple-promoter system.
Shibukawa, Y., et al., J. Biol. Chem. 278(5):3197-3203 (2003).Koyama, N., et al., Eur. J. Biochem. 238(3):853-861 (1996).Kim, Y.J., et al., Gene 170(2):281-283 (1996).Ihara, Y., et al., J. Biochem. 113(6):692-698 (1993).
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