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Mouse Anti-FUT5 Recombinant Antibody (CBXF-3240) (CBMAB-F3934-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-3240
Antibody Isotype
IgG2b, κ
Application
ELISA, WB

Basic Information

Immunogen
Partial recombinant corresponding to aa95-164 from human FUT5 (NP_002025) 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.

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
2527
UniProt ID
Q11128
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.

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