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FUT5 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q11128 |
|---|---|
| Clone Names | 91009135 |
| Gene ID | 2527 |
|---|---|
| Other Names | Alpha-(1, 3)-fucosyltransferase 5, Fucosyltransferase 5, Fucosyltransferase V, Fuc-TV, FucT-V, Galactoside 3-L-fucosyltransferase, FUT5 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP9296c was selected from the Center region of human FUT5. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | FUT5 (HGNC:4016) |
|---|---|
| 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:7721776, PubMed:9737988, PubMed:17604274, PubMed:9737989, PubMed:29593094). 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 oligosaccharide via an alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:7721776, PubMed:9737988, PubMed:17604274). 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 |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
FUT5 may catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens.
References
Norden,R., et.al, Glycobiology 19 (7), 776-788 (2009)Chiu,P.C., et.al, J. Cell. Sci. 120 (PT 1), 33-44 (2007)Inaba,Y., et.al, Int. J. Cancer 107 (6), 949-957 (2003)
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