|Other Names||Polypeptide N-acetylgalactosaminyltransferase 6, Polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, Protein-UDP acetylgalactosaminyltransferase 6, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, GALNT6|
|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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Expressed in placenta and trachea. Weakly expressed in brain and pancreas. Expressed in fibroblast. Weakly or not expressed in lung, liver, muscle, kidney, spleen, thymus, prostate, testis, ovary, intestine, colon, leukocyte, stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland and bone marrow.|
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Provided below are standard protocols that you may find useful for product applications.
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. The encoded protein is capable of glycosylatingfibronectin peptide in vitro and is expressed in a fibroblast cellline, indicating that it may be involved in the synthesis ofoncofetal fibronectin.
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Gomes, J., et al. J. Histochem. Cytochem. 57(1):79-86(2009)Patani, N., et al. Cancer Genomics Proteomics 5(6):333-340(2008)Argueso, P., et al. Invest. Ophthalmol. Vis. Sci. 44(1):86-92(2003)Bennett, E.P., et al. J. Biol. Chem. 274(36):25362-25370(1999)
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