Recombinant Human FUT3 protein (denatured)
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Recombinant Human FUT3 protein (denatured) is a Human Fragment protein, in the 35 to 361 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.
View Alternative Names
FT3B, LE, FUT3, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3, 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, Alpha-3-fucosyltransferase FUT3, Blood group Lewis alpha-4-fucosyltransferase, Fucosyltransferase 3, Fucosyltransferase III, Lewis FT, FucT-III
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human FUT3 protein (denatured) (AB171721)
15% SDS-PAGE analysis of ab171721 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
FUT3 contributes to the formation of fucosylated oligosaccharide structures on glycoproteins and glycolipids. It is not strictly part of a multi-protein complex but works closely intertwined with other glycosyltransferases for effective oligosaccharide biosynthesis. FUT3's activity influences cell-cell recognition and signaling processes by modifying cell surface carbohydrate structures.
Pathways
FUT3 is heavily involved in glycosphingolipid biosynthesis and the metabolic pathway of glycan structures. FUT3 works together with other fucosyltransferases such as FUT1 and FUT2 in these pathways dictating the structural diversity and functionality of various glycoconjugates. These pathways are important for cellular interactions and communication impacting blood group antigen expression.
Specifications
Form
Liquid
Additional notes
ab17121 was purified by anion-exchange and gel-filtration chromatography techniques.
General info
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).
Sequence similarities
Belongs to the glycosyltransferase 10 family.
Post-translational modifications
Glycosylated.
Target data
Product promise
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