Recombinant Mouse Alpha- (FUT7) Protein (His&Myc)
Beta LifeScience
SKU/CAT #: BLC-10922P
Greater than 90% as determined by SDS-PAGE.
Recombinant Mouse Alpha- (FUT7) Protein (His&Myc)
Beta LifeScience
SKU/CAT #: BLC-10922P
Collections: Other recombinant proteins, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
| Description | Recombinant Mouse Alpha- (FUT7) Protein (His&Myc) is produced by our Mammalian cell expression system. This is a protein fragment. |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Uniprotkb | Q11131 |
| Target Symbol | FUT7 |
| Synonyms | Fut7Alpha-(1,3)-fucosyltransferase 7; EC 2.4.1.-; Fucosyltransferase 7; Fucosyltransferase VII; Fuc-TVII; FucT-VII; Galactoside 3-L-fucosyltransferase |
| Species | Mus musculus (Mouse) |
| Expression System | Mammalian cell |
| Tag | N-10His&C-Myc |
| Target Protein Sequence | LWGSAPGSAPVPQSTLTILIWHWPFTNRPPELPGDTCTRYGMASCRLSANRSLLASADAVVFHHRELQTRQSLLPLDQRPHGQPWVWASMESPSNTHGLHRFRGIFNWVLSYRRDSDIFVPYGRLEPLSGPTSPLPAKSRMAAWVISNFQERQQRAKLYRQLAPHLQVDVFGRASGRPLCANCLLPTLARYRFYLAFENSQHRDYITEKFWRNALAAGAVPVALGPPRATYEAFVPPDAFVHVDDFSSARELAVFLVSMNESRYRGFFAWRDRLRVRLLGDWRERFCTICARYPYLPRSQVYEDLESWFQA |
| Expression Range | 79-389aa |
| Protein Length | Partial |
| Mol. Weight | 40.9 kDa |
| Research Area | Developmental Biology |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
| Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
| Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
| Target 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 upregulating 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. |
| Subcellular Location | Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. |
| Protein Families | Glycosyltransferase 10 family |
| Database References | |
| Tissue Specificity | Highly expressed in lung and bone marrow and to a much lesser extent in spleen, salivary gland and skeletal muscle. |
Gene Functions References
- The DNA demethylation within the fut7 gene controls selectin ligand expression in mice, including the inducible topographic commitment of T cells for skin and inflamed sites. PMID: 27591321
- Cloning of an intragenic region spanning a 1kb region upstream of exon 4 into an enhancer-containing vector indeed elicited fut7 promoter activity in cd4 positive T cells. PMID: 24915132
- These results demonstrate that all genetic information essential for appropriate and selective expression of Fut7 in diverse cell types and in response to distinct developmental signals is contained within this comparatively small genetic region. PMID: 24459148
- alpha(1,3)-Fucosyltransferases FUT4 and FUT7 control murine susceptibility to thrombosis. PMID: 23562273
- striking differences between the requirement of FucT-VII and C2GlcNAcT-I for Ligands for E-selectin and P-selectin expression in CD4+ T cells. PMID: 23039181
- Loss of the barrier protective molecule TFF3 leads to a profound increase in susceptibility to DSS-induced colitis, and this can be abrogated by reducing Fuc-TVII-dependent leukocyte recruitment. PMID: 20299601
- FucT-VII is an important pathophysiologic mediator of renal ischemia reperfusion injury, structural damage, and neutrophil infiltration postischemia. PMID: 12193737
- Efficient recruitment of activated lymphocytes to the brain in a model mimicking early inflammation during experimental allergic encephalomyelitis is controlled by FucT-VII. PMID: 15843584
- Keratan sulfate sulfotransferase competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation. PMID: 17172261
- a deficiency in Fuc-TVII, and in a more pronounced fashion, a combined deficiency in both Fuc-TIV and Fuc-TVII, leads to accelerated death following M. tuberculosis infection PMID: 19608009
