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GALNT2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q10471 |
|---|
| Gene ID | 2590 |
|---|---|
| Other Names | Polypeptide N-acetylgalactosaminyltransferase 2, Polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, Protein-UDP acetylgalactosaminyltransferase 2, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, Polypeptide N-acetylgalactosaminyltransferase 2 soluble form, GALNT2 |
| 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 | GALNT2 |
|---|---|
| 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 a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism (PubMed:27508872, PubMed:32293671). |
| Cellular Location | Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists |
| Tissue Location | Detected in urine (at protein level) (PubMed:37453717). Widely expressed. |
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Provided below are standard protocols that you may find useful for product applications.
Background
GALNT2 encodes polypeptide N-acetylgalactosaminyltransferase 2, 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 in a cell is regulated by a repertoire of GalNAc-transferases.
References
Weissglas-Volkov,D. Circ Cardiovasc Genet 3 (1), 31-38 (2010)Hegele,R.A. Hum. Mol. Genet. 18 (21), 4189-4194 (2009)Nakayama,K. J. Med. Genet. 46 (6), 370-374 (2009)
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