Analytical Data
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Gene name
FUT6
- Application
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Alternative Names
FT1A; FCT3A; FucT-VI; Alpha-(1,3)-Fucosyltransferase; Galactoside 3-L-Fucosyltransferase
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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
P51993
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Expression Region
Arg35~Thr359
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Molecular Weight
40kDa
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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
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Protein Description
FUT6, known as fucosyltransferase 6, is a glycosyltransferase enzyme that plays a critical role in the addition of fucose residue to glycoproteins and glycolipids. This enzymatic activity is vital for various biological processes, including cellular signaling, immune response, and development. The study of FUT6 is particularly significant in the context of cancer and other diseases where altered glycosylation patterns are observed. Research has indicated that elevated levels of FUT6 expression are associated with tumor progression and metastasis, making it a potential biomarker and therapeutic target. Additionally, the functional mechanisms of FUT6 and its interactions with other glycosyltransferases have garnered attention, highlighting the complexity of glycan biosynthesis. Recombination technology has enabled researchers to produce recombinant FUT6 protein, facilitating in-depth studies of its structure-function relationships and biochemical properties. By isolating and characterizing FUT6, scientists aim to gain insights into its role in pathological conditions and explore its potential applications in diagnostic and therapeutic strategies. Understanding FUT6’s biochemical pathways could pave the way for innovative treatments targeting aberrant glycosylation, further emphasizing its importance in biomedical research.
