|Other Names||Polypeptide N-acetylgalactosaminyltransferase 9, Polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, Protein-UDP acetylgalactosaminyltransferase 9, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, GALNT9|
|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||Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Does not glycosylate apomucin or SDC3.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Specifically expressed in brain. Not expressed in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. In brain, it is expressed in cerebellum, frontal lobe, temporal lobe, putamen and spinal cord, weakly expressed in cerebral cortex. Not expressed in medulla and occipital pole.|
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This gene encodes a member of theUDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes.GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgiapparatus by catalyzing the transfer of GalNAc to serine andthreonine residues on target proteins. They are characterized by anN-terminal transmembrane domain, a stem region, a lumenal catalyticdomain containing a GT1 motif and Gal/GalNAc transferase motif, anda C-terminal ricin/lectin-like domain. GalNAc-Ts have different,but overlapping, substrate specificities and patterns ofexpression. This gene is expressed specifically in the brain, withhighest expression in the cerebellum. Multiple transcript variantsencoding different isoforms have been found for this gene.
Wang, A.G., et al. Biochem. Biophys. Res. Commun. 345(3):1022-1032(2006)Zhang, Y., et al. J. Biol. Chem. 278(1):573-584(2003)Toba, S., et al. Biochim. Biophys. Acta 1493 (1-2), 264-268 (2000) :
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