

| Catalog No. | HD175012 |
|---|---|
| Description |
Recombinant Human FUT7 Protein, N-His (HD175012) expressed in E. coli, spanning Pro37-Ala342. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q11130 |
| Protein length | Pro37-Ala342 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 37.81 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | Alpha-(1,3)-fucosyltransferase 7, EC:2.4.1.-, FUT7, Fuc-TVII, FucT-VII, Fucosyltransferase 7, Fucosyltransferase VII, Galactoside 3-L-fucosyltransferase, Selectin ligand synthase |
| Background | Alpha-(1,3)-fucosyltransferase 7 is a ~39 kDa protein. Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. 1. Bengtson, P. et al. (2001) The Journal of biological chemistry 276, 31575-82. PMID: 11404359 2. Miyashiro, M. et al. (2004) Journal of biochemistry 136, 723-31. PMID: 15632313 3. Prorok-Hamon, M. et al. (2005) The Biochemical journal 391, 491-502. PMID: 15926890 4. Zhang, Y. et al. (2009) Fertility and sterility 91, 908-14. PMID: 18402946 5. Liu, S. et al. (2008) IUBMB life 60, 461-6. PMID: 18553500 6. Mondal, N. et al. (2018) The Journal of biological chemistry 293, 7300-7314. PMID: 29593094 7. Natsuka, S. et al. (1994) The Journal of biological chemistry 269, 16789-94. PMID: 8207002 8. Knibbs, RN. et al. (1996) The Journal of cell biology 133, 911-20. PMID: 8666674 9. Malý, P. et al. (1996) Cell 86, 643-53. PMID: 8752218 10. Stroud, MR. et al. (1997) Biochemical and biophysical research communications 238, 165-8. PMID: 9299472 |
| Note | For research use only |
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