Analytical Data
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Gene name
FUT5
- Application
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Alternative Names
FUC-TV; Galactoside 3-L-fucosyltransferase; Alpha-(1,3)-fucosyltransferase 5
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q11128
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Expression Region
Arg35~Thr374
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Molecular Weight
43kDa
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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
FUT5, or Fucosyltransferase 5, is an enzyme belonging to the fucosyltransferase family, which is crucial for synthesizing fucosylated glycans. These glycans play significant roles in various biological processes, including cell adhesion, immune response, and pathogenesis in diseases such as cancer. The interest in FUT5 research stems from its implications in cell signaling and its potential as a biomarker for disease progression. Additionally, fucosylated glycans are involved in the modulation of stem cell behavior and cancer metastasis, making FUT5 a significant target for therapeutic interventions. Understanding the structure, function, and regulation of FUT5 may provide insights into its role in glycan biosynthesis, leading to novel strategies for disease diagnosis and treatment. Recent advances in biotechnology have enabled the production and characterization of recombinant FUT5, allowing detailed studies into its enzymatic mechanisms and functional effects in cellular contexts. This research not only enhances our knowledge of glycosylation but also paves the way for potential applications in medicine and biotechnology, underscoring the importance of FUT5 in both fundamental and applied sciences.
