|Other Names||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Beta-1, 3-glucuronyltransferase 3, Glucuronosyltransferase I, GlcAT-I, UDP-GlcUA:Gal beta-1, 3-Gal-R glucuronyltransferase, GlcUAT-I, B3GAT3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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||Glycosaminoglycans biosynthesis (PubMed:25893793). Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4- Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1- 4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation (PubMed:24425863).|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein. Golgi apparatus, cis-Golgi network|
|Tissue Location||Ubiquitous (but weakly expressed in all tissues examined)|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is a member of theglucuronyltransferase gene family, enzymes that exhibit strictacceptor specificity, recognizing nonreducing terminal sugars andtheir anomeric linkages. This gene product catalyzes the formationof the glycosaminoglycan-protein linkage by way of a glucuronyltransfer reaction in the final step of the biosynthesis of thelinkage region of proteoglycans.
Tone, Y., et al. J. Biol. Chem. 283(24):16801-16807(2008)Fondeur-Gelinotte, M., et al. Glycobiology 17(8):857-867(2007)Lamesch, P., et al. Genomics 89(3):307-315(2007)Gulberti, S., et al. J. Biol. Chem. 280(2):1417-1425(2005)Venkatesan, N., et al. Proc. Natl. Acad. Sci. U.S.A. 101(52):18087-18092(2004)
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