|Other Names||Polypeptide N-acetylgalactosaminyltransferase 15, Polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, Polypeptide N-acetylgalactosaminyltransferase-like protein 2, Protein-UDP acetylgalactosaminyltransferase-like protein 2, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, GALNT15, GALNTL2|
|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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Widely expressed. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage.|
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Provided below are standard protocols that you may find useful for product applications.
GALNTL2 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.
Cheng,L. FEBS Lett. 566 (1-3), 17-24 (2004)Clark,H.F. Genome Res. 13 (10), 2265-2270 (2003)Kumar,S. Osteoarthr. Cartil. 9 (7), 641-653 (2001)
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