FUT3 antibody - C-terminal region
Rabbit Polyclonal Antibody
- 产品详情
- 实验流程
Application ![]()
| WB |
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Primary Accession | P21217 |
Other Accession | NM_000149, NP_000140 |
Reactivity | Human, Pig |
Predicted | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 42117 Da |
Gene ID | 2525 |
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Alias Symbol | CD174, FT3B, FucT-III, LE, Les, MGC131739 |
Other Names | Galactoside 3(4)-L-fucosyltransferase, 2.4.1.65, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE |
Format | Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. |
Reconstitution & Storage | Add 50 ul of distilled water. Final anti-FUT3 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at 20°C. Avoid repeat freeze-thaw cycles. |
Precautions | FUT3 antibody - C-terminal region is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | FUT3 (HGNC:4014) |
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Synonyms | FT3B, LE |
Function | Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D- GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors (PubMed:11058871, PubMed:12668675, PubMed:1977660). Through its catalytic activity, participates in the synthesis of antigens of the Lewis blood group system, i.e. Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed:11058871, PubMed:12668675, PubMed:1977660). Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sLe(a) expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed:11058871, PubMed:12668675, PubMed:27453266). Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed:11058871, PubMed:29593094). Prefers type 1 chain over type 2 acceptors (PubMed:7721776). Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed:7721776). Lewis- positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme (PubMed:1977660). |
Cellular Location | Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein Note=Membrane-bound form in trans cisternae of Golgi |
Tissue Location | Highly expressed in stomach, colon, small intestine, lung and kidney and to a lesser extent in salivary gland, bladder, uterus and liver. |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
REFERENCES
Kukowska-Latallo J.F.,et al.Genes Dev. 4:1288-1303(1990).
Cameron H.S.,et al.J. Biol. Chem. 270:20112-20122(1995).
Rahim I.,et al.Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
Matzhold E.M.,et al.Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
Grimwood J.,et al.Nature 428:529-535(2004).

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