GALNT14 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q96FL9 |
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Clone Names | 110717062 |
Gene ID | 79623 |
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Other Names | Polypeptide N-acetylgalactosaminyltransferase 14, Polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, Protein-UDP acetylgalactosaminyltransferase 14, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, GALNT14 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | GALNT14 |
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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. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney. |
Cellular Location | Golgi apparatus membrane; Single- pass type II membrane protein |
Tissue Location | Detected in renal tubules (at protein level). Highly expressed in fetal and adult kidney. Widely expressed at low level. Weakly expressed in whole brain, cerebellum, thymus, lung, mammary gland, liver, stomach, small intestine, colon, pancreas, spleen, bladder, uterus, placenta, testis, ovary, skeletal muscle, leukocyte, B-cell, bone marrow, fetal brain, fetal thymus, fetal lung, fetal liver, fetal small intestine, fetal spleen, fetal skeletal and fetus. Detected in renal tubules (at protein level) |
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Provided below are standard protocols that you may find useful for product applications.
Background
GALNT14 (EC 2.4.1.41) belongs to a large subfamily ofglycosyltransferases residing in the Golgi apparatus. GALNT enzymescatalyze the first step in the O-glycosylation of mammalianproteins by transferring N-acetyl-D-galactosamine (GalNAc) topeptide substrates.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Stern, H.M., et al. Clin. Cancer Res. 16(5):1587-1596(2010)Wu, C., et al. BMC Cancer 10, 123 (2010) :Wu, C., et al. J. Biosci. 34(3):389-395(2009)Wu, C., et al. Biochem. Biophys. Res. Commun. 357(2):360-365(2007)
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