FUT5 Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
Application ![]()
| IHC-P, IHC-F, IF, ICC, E |
---|---|
Primary Accession | Q11128 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 42989 Da |
Physical State | Liquid |
Immunogen | KLH conjugated synthetic peptide derived from human FUT5 |
Epitope Specificity | 281-374/374 |
Isotype | IgG |
Purity | affinity purified by Protein A |
Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
SUBCELLULAR LOCATION | Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. |
SIMILARITY | Belongs to the glycosyltransferase 10 family. |
Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
Background Descriptions | The protein encoded by this gene belongs to the glycosyltransferase family. It is localized to the golgi, and catalyzes the last step in the biosynthesis of Lewis X (LeX) antigen, the addition of a fucose to precursor polysaccharides. This protein is one of the few fucosyltransferases that synthesizes the LeX oligosaccharide (CD15) expressed in the organ buds progressing in mesenchyma during embryogenesis. It is also responsible for the expression of CD15 in mature granulocytes. A common haplotype of this gene has also been associated with susceptibility to placental malaria infection. [provided by RefSeq, Nov 2011] |
Gene ID | 2527 |
---|---|
Other Names | 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5, 2.4.1.152, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5, 2.4.1.65, Fucosyltransferase 5, Fucosyltransferase V, Fuc-TV, FucT-V, Galactoside 3-L-fucosyltransferase, FUT5 (HGNC:4016) |
Target/Specificity | Liver, colon and testis and trace amounts in T-cells and brain. |
Dilution | IHC-P=1:100-500,IHC-F=1:100-500,ICC=1:100-500,IF=1:100-500,ELISA=1:5000-10000 |
Format | 0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce |
Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
Name | FUT5 (HGNC:4016) |
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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). |
Cellular Location | Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi |
Tissue Location | Liver, colon and testis and trace amounts in T- cells and brain |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.
Application Protocols
Provided below are standard protocols that you may find useful for product applications.

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