MGAT2 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
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Primary Accession | Q10469 |
Other Accession | Q09326, O19071, Q921V5, NP_002399 |
Reactivity | Human |
Predicted | Mouse, Pig, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 51550 Da |
Antigen Region | 409-439 aa |
Gene ID | 4247 |
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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 | This MGAT2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 409-439 amino acids from the C-terminal region of human MGAT2. |
Dilution | WB~~1:1000 FC~~1:10~50 |
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 | MGAT2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | MGAT2 |
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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 |
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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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