Analytical Data
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Gene name
FUT7
- Application
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Alternative Names
FUT7;Alpha-(1.3)-fucosyltransferase 7
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q11130
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Expression Region
37-342aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSPRGTPAPQPTITILVWHWPFTDQPPEL PSDTCTRYGIARCHLSANRSLLASADAVVFHHRELQTRRSHLPLAQRPRG QPWVWASMESPSHTHGLSHLRGIFNWVLSYRRDSDIFVPYGRLEPHWGPS PPLPAKSRVAAWVVSNFQERQLRARLYRQLAPHLRVDVFGRANGRPLCAS CLVPTVAQYRFYLSFENSQHRDYITEKFWRNALVAGTVPVVLGPPRATYE AFVPADAFVHVDDFGSARELAAFLTGMNESRYQRFFAWRDRLRVRLFTDW RERFCAICDRYPHLPRSQVYEDLEGWFQA
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Molecular Weight
38 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FUT7, or fucosyltransferase 7, is an important enzyme involved in the biosynthesis of fucosylated glycans, which play critical roles in various biological processes such as cell adhesion, immune response, and cancer metastasis. Research on FUT7 has gained traction due to its implications in several pathological conditions, including inflammatory diseases and tumor progression. The enzyme catalyzes the transfer of fucose, a sugar, to glycoproteins and glycolipids, influencing molecular interactions and signaling pathways. Abnormal expression of FUT7 has been linked to the enhanced invasiveness of cancer cells, making it a potential biomarker for cancer diagnosis and a target for therapeutic intervention. Studies have explored the structure, function, and regulation of FUT7, as well as its role in modulating the tumor microenvironment. Furthermore, recombinant FUT7 proteins have been utilized in various assays aimed at understanding fucosylation's impact on cellular behaviors. As the understanding of FUT7's functions expands, so does the potential for developing novel strategies to manipulate fucosylation for therapeutic purposes, highlighting the enzyme's relevance in both basic research and clinical applications. Consequently, FUT7 remains a focal point of ongoing studies aimed at uncovering the complexities of glycosylation and its broader implications in health and disease.
