Recombinant Mouse Alpha- (1,3)-fucosyltransferase 7 (Fut7), partial

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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Developmental Biology
Alternative Names
Fucosyltransferase 7 (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase)
Mus musculus (Mouse)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
62.5 kDa
Protein Length
Tag Info
N-terminal GST-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

Discover our Recombinant Mouse Fut7 protein, meticulously engineered for researchers focused on developmental biology and glycosylation studies. This protein features the Alpha-(1,3)-fucosyltransferase 7 enzyme, also known as Fucosyltransferase 7 and Galactoside 3-L-fucosyltransferase, responsible for catalyzing the transfer of L-fucose residues to various glycoproteins and glycolipids, playing a crucial role in cell adhesion and signaling processes during development.

Synthesized in an E. coli expression system, our Mouse Fut7 protein covers a partial length of the enzyme with an expression range of 79-389aa. The N-terminal GST-tag facilitates efficient purification and detection methods, ensuring a streamlined research experience. With a purity greater than 85% as determined by SDS-PAGE, our recombinant protein is available in both liquid and lyophilized powder forms to accommodate different experimental needs.

Choose our precision-crafted Recombinant Mouse Fut7 protein for consistent and dependable results in your developmental biology and glycosylation research projects.

Customer Reviews and Q&A

 Customer Reviews
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Applications : Western blot assays

Review: Western blotting analysis of HECA452 expression of FTVII-unmodifed BMSCs and FTVII-modifed BMSCs, the positive bands were at~70KD and~35KD.

By Anonymous

Target Background

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.
Gene References into Functions
  1. 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
  2. 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
  3. 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
  4. alpha(1,3)-Fucosyltransferases FUT4 and FUT7 control murine susceptibility to thrombosis. PMID: 23562273
  5. 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
  6. 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
  7. FucT-VII is an important pathophysiologic mediator of renal ischemia reperfusion injury, structural damage, and neutrophil infiltration postischemia. PMID: 12193737
  8. 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
  9. 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
  10. 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

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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
Tissue Specificity
Highly expressed in lung and bone marrow and to a much lesser extent in spleen, salivary gland and skeletal muscle.
Database Links
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