|Other Names||Polypeptide N-acetylgalactosaminyltransferase 13, Polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, Protein-UDP acetylgalactosaminyltransferase 13, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, GALNT13, KIAA1918|
|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. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Specifically expressed in neuronal cells. Expressed in fetal brain, whole adult brain, cerebral cortex and cerebellum. Not expressed in other tissues tested|
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Provided below are standard protocols that you may find useful for product applications.
The GALNT13 protein is a member of theUDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase (GalNAcT; EC 184.108.40.206) family,which initiate O-linked glycosylation of mucins (see MUC3A, MIM158371) by the initial transfer of N-acetylgalactosamine (GalNAc)with an alpha-linkage to a serine or threonine residue.[supplied byOMIM].
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Ng, D., et al. Int. J. Cancer 123(7):1610-1615(2008)Lunetta, K.L., et al. BMC Med. Genet. 8 SUPPL 1, S13 (2007) :Hillier, L.W., et al. Nature 434(7034):724-731(2005)Lehner, B., et al. Genome Res. 14(7):1315-1323(2004)
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