Human Fucosyltransferase 7/FUT7 protein (Recombinant) (His-Tag) (STJP018721)
SPECIFICATIONS
HostE.coli
ImmunogenHuman
General Information
| Short Description | Recombinant-Human Fucosyltransferase 7/FUT7-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | SDS-PAGE/Denatured |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 0.25 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M urea, 10% Glycerol |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | FUT7 |
| Gene ID | 2529 |
| Uniprot ID | FUT7_HUMAN |
| Accession Number | NP_004470 |
| Immunogen | Human |
| Immunogen Region | 37-342aa |
| Immunogen Sequence | MGSSHHHHHH SSGLVPRGSH MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKF |
Additional Info
| Tissue Specificity | Leukocytic/myeloid lineage cells. |
| Post Translational Modifications | N-glycosylated. |
| Function | 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. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit. |
| Protein Name | Alpha-(1 -3-Fucosyltransferase 7Fucosyltransferase 7Fucosyltransferase ViiFuc-TviiFuct-ViiGalactoside 3-L-FucosyltransferaseSelectin Ligand Synthase |
| Database Links | Reactome: R-HSA-9037629 |
| Cellular Localisation | Golgi ApparatusGolgi Stack MembraneSingle-Pass Type Ii Membrane ProteinMembrane-Bound Form In Trans Cisternae Of Golgi |
| Alternative Protein Names | Alpha-(1 -3-Fucosyltransferase 7 proteinFucosyltransferase 7 proteinFucosyltransferase Vii proteinFuc-Tvii proteinFuct-Vii proteinGalactoside 3-L-Fucosyltransferase proteinSelectin Ligand Synthase proteinFUT7 protein |
Information sourced from Uniprot.org