|Other Names||Polypeptide N-acetylgalactosaminyltransferase 3, Polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, Protein-UDP acetylgalactosaminyltransferase 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, GALNT3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP9208c was selected from the Center region of human GALNT3. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|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. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis.|
|Cellular Location||Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Resides preferentially in the trans and medial parts of the Golgi stack|
|Tissue Location||Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon Also expressed in placenta and lung and fetal lung and fetal kidney.|
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Provided below are standard protocols that you may find useful for product applications.
GALNT3 encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein is highly homologous to other family members, however the enzymes have different substrate specificities.
Joseph,L., et.al., Skeletal Radiol. 39 (1), 63-68 (2010)Masi,L.,et.al., J Bone Joint Surg Am 91 (5), 1190-1198 (2009)Chefetz,I., et.al, Biochim. Biophys. Acta 1792 (1), 61-67 (2009)
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