Recombinant Human FUT5 protein
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Recombinant Human FUT5 protein is a Human Fragment protein, in the 203 to 374 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5, Fucosyltransferase 5, Fucosyltransferase V, Galactoside 3-L-fucosyltransferase, Fuc-TV, FucT-V, FUT5
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human FUT5 protein (AB80076)
SDS PAGE analysis , 20% gel (Commassie blue staining) showing ab80076 at approximately 30kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
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
FUT5 contributes to the modification of glycoproteins and glycolipids impacting cellular adhesion and signaling mechanisms. This enzyme forms part of a biosynthetic complex involved in the creation of specific fucosylated structures. These structures participate in immune responses and development. FUT5 collaborates closely with other members of the fucosyltransferase enzyme family to determine glycan structures present on cell surfaces.
Pathways
FUT5 participates in the glycosphingolipid biosynthesis pathway and the protein glycosylation pathway. These pathways are important for cell communication and immune recognition. It collaborates with proteins like FUT3 and FUT6 sharing functional and structural similarities within these pathways. The glycosylation process involves multiple enzymes which ensure accurate structural formation of glycoproteins necessary for physiological processes.
Specifications
Form
Lyophilized
General info
Function
Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosaccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens (PubMed : 14718375, PubMed : 1740457, PubMed : 17604274, PubMed : 29593094, PubMed : 7721776, PubMed : 9737988, PubMed : 9737989). Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate (PubMed : 17604274, PubMed : 7721776). Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an alpha (1,4) linkage (PubMed : 14718375, PubMed : 1740457, PubMed : 17604274, PubMed : 7721776, PubMed : 9737988). Preferentially catalyzes sialylated type 2 oligosaccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide acceptors (PubMed : 1740457, PubMed : 9737989). Lactose-based structures are also acceptor substrates (PubMed : 1740457, PubMed : 7721776).
Sequence similarities
Belongs to the glycosyltransferase 10 family.
Target data
Complementary Products
Product promise
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