• Western blot analysis of various lysates using FUT3 Rabbit polyclonal antibody (STJ117252) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (STJS000856) at 1:10000 dilution. Lysates/proteins: 25 Mu g per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit. Exposure time: 90s.

Anti-FUT3 antibody (1-100) (STJ117252)

SKU:
STJ117252

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Host: Rabbit
Applications: WB
Reactivity: Human/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-FUT3 (1-100) is suitable for use in Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.01% Thimerosal, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:500-1:2000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: FUT3
Gene ID: 2525
Uniprot ID: FUT3_HUMAN
Immunogen Region: 1-100
Immunogen: A synthetic peptide corresponding to a sequence within amino acids 1-100 of human FUT3 (NP_000140.1).
Immunogen Sequence: MDPLGAAKPQWPWRRCLAAL LFQLLVAVCFFSYLRVSRDD ATGSPRAPSGSSRQDTTPTR PTLLILLWTWPFHIPVALSR CSEMVPGTADCHITADRKVY
Tissue Specificity Highly expressed in stomach, colon, small intestine, lung and kidney and to a lesser extent in salivary gland, bladder, uterus and liver.
Post Translational Modifications Glycosylated.
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 and participates in the blood groups Lewis determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens. 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 sialyl Lewis a expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration. 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. Prefers type 1 chain over type 2 acceptors. Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred. Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme.
Protein Name 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
Lewis Ft
Fucosyltransferase 3
Fucosyltransferase Iii
Fuct-Iii
Database Links Reactome: R-HSA-9037629
Reactome: R-HSA-975578
Cellular Localisation Golgi Apparatus
Golgi Stack Membrane
Single-Pass Type Ii Membrane Protein
Membrane-Bound Form In Trans Cisternae Of Golgi
Alternative Antibody Names Anti-3-Galactosyl-N-Acetylglucosaminide 4-Alpha-L-Fucosyltransferase Fut3 antibody
Anti-4-Galactosyl-N-Acetylglucosaminide 3-Alpha-L-Fucosyltransferase antibody
Anti-Alpha-3-Fucosyltransferase Fut3 antibody
Anti-Blood Group Lewis Alpha-4-Fucosyltransferase antibody
Anti-Lewis Ft antibody
Anti-Fucosyltransferase 3 antibody
Anti-Fucosyltransferase Iii antibody
Anti-Fuct-Iii antibody
Anti-FUT3 antibody
Anti-FT3B antibody
Anti-LE antibody

Information sourced from Uniprot.org

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