|Application ||WB, E|
|Calculated MW||68919 Da|
|Antigen Region||110-138 aa|
|Other Names||Polypeptide N-acetylgalactosaminyltransferase 11, Polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, Protein-UDP acetylgalactosaminyltransferase 11, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, GALNT11|
|Target/Specificity||This GLT11 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 110-138 amino acids from the N-terminal region of human GLT11.|
|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||GLT11 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N- acetylgalactosaminyltransferases catalyze the transfer of an N- acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO).|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Highly expressed in kidney. Expressed at intermediate level in brain, heart and skeletal muscle. Weakly expressed other tissues. In kidney, it is strongly expressed in tubules but not expressed in glomeruli|
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Provided below are standard protocols that you may find useful for product applications.
GALNT11 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. Displays the same enzyme activity toward Muc1, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin.
Yuasa, I., et al. Leg Med (Tokyo) 12(4):208-211(2010)
Schwientek, T., et al. J. Biol. Chem. 277(25):22623-22638(2002)
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