Mouse Anti-FUT5 Recombinant Antibody (CBXF-0962) (CBMAB-F3221-CQ)

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Basic Information

Host Animal
Mouse
Clone
CBXF-0962
Application
S-ELISA, ELISA, WB
Immunogen
FUT5 (NP_002025, 95 a.a.-164 a.a) partial recombinant protein with GST tag
Specificity
Human
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

Target

Full Name
fucosyltransferase 5 (alpha (1,3) fucosyltransferase)
Introduction
FUT5 (Fucosyltransferase 5) is a Protein Coding gene. Among its related pathways are Metabolism and Glycosphingolipid biosynthesis - lacto and neolacto series. Gene Ontology (GO) annotations related to this gene include fucosyltransferase activity and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity. An important paralog of this gene is FUT3.
Entrez Gene ID
UniProt ID
Alternative Names
Fucosyltransferase 5; Galactoside 3-L-Fucosyltransferase; Alpha (1,3) Fucosyltransferase; Fucosyltransferase V; EC 2.4.1.65; FUC-TV; FucT-V; Alpha-(1,3)-Fucosyltransferase 5; EC 2.4.1;
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 oligosacccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface espression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens (PubMed:14718375, PubMed:1740457, PubMed:7721776, PubMed:9737988, PubMed:17604274, PubMed:9737989).

Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate (PubMed:7721776, PubMed:17604274).

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 oligosacccharide via an alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:7721776, PubMed:9737988, PubMed:17604274).

Preferentially catalyzes sialylated type 2 oligosacccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosacccharide acceptors (PubMed:1740457, PubMed:9737989).

Lactose-based structures are also acceptor substrates (PubMed:1740457, PubMed:7721776).
Biological Process
Carbohydrate metabolic process Source: ProtInc
Ceramide metabolic process Source: UniProtKB
Fucosylation Source: GO_Central
L-fucose catabolic process Source: UniProtKB
Oligosaccharide biosynthetic process Source: Reactome
Oligosaccharide metabolic process Source: UniProtKB
Protein glycosylation Source: UniProtKB
Cellular Location
Golgi stack membrane. Membrane-bound form in trans cisternae of Golgi.
Topology
Cytoplasmic: 1-15
Helical: 16-34
Lumenal: 35-374
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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