|Other Names||N-acetylgalactosaminyltransferase 7, 241-, Polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, Protein-UDP acetylgalactosaminyltransferase 7, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, GALNT7|
|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||Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS|
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Provided below are standard protocols that you may find useful for product applications.
GALNT7 is GalNAc transferase 7, a member of theGalNAc-transferase family. The enzyme encoded by this gene controlsthe initiation step of mucin-type O-linked protein glycosylationand transfer of N-acetylgalactosamine to serine and threonine aminoacid residues. This enzyme is a type II transmembrane protein andshares common sequence motifs with other family members. Unlikeother family members, this enzyme shows exclusive specificity forpartially GalNAc-glycosylated acceptor substrates and shows noactivity with non-glycosylated peptides. This protein may functionas a follow-up enzyme in the initiation step of O-glycosylation.
Kahai, S., et al. PLoS ONE 4 (10), E7535 (2009) :Bennett, E.P., et al. FEBS Lett. 460(2):226-230(1999)
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