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MGAT2 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q10469 |
|---|---|
| Other Accession | NP_002399 |
| Clone Names | 3102223 |
| Gene ID | 4247 |
|---|---|
| Other Names | Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, Beta-1, 2-N-acetylglucosaminyltransferase II, GlcNAc-T II, GNT-II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II, MGAT2 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2407b was selected from the C-term region of human MGAT2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| 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 | MGAT2 |
|---|---|
| Function | Plays an essential role in protein N-glycosylation. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans. |
| Cellular Location | Golgi apparatus membrane; Single-pass type II membrane protein |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
MGAT2 (UDP-N-acetylglucosamine:alpha-6-D-mannoside-beta-1, 2-N-acetylglucosaminyltransferase II) is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in MGAT2 may lead to carbohydrate-deficient glycoprotein syndrome, type II.
References
Yen, C.L., et al., J. Biol. Chem. 278(20):18532-18537 (2003).Chen, S.H., et al., Glycoconj. J. 15(3):301-308 (1998).Tan, J., et al., Am. J. Hum. Genet. 59(4):810-817 (1996).Tan, J., et al., Eur. J. Biochem. 231(2):317-328 (1995).D'Agostaro, G.A., et al., J. Biol. Chem. 270(25):15211-15221 (1995).
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