|Application ||WB, E|
|Other Accession||Q5EA41, NP_009141.2|
|Calculated MW||71159 Da|
|Antigen Region||552-579 aa|
|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|
|Target/Specificity||This GALNT6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 552-579 amino acids from the C-terminal region of human GALNT6.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GALNT6 Antibody (C-term) is for research use only and 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 the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal 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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