Analytical Data
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Gene name
FUT3
- Application
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Alternative Names
CD174; FUT3; FT3B; LE; Les; FucT-III; Lewis FT; Galactoside 3(4)-L-Fucosyltransferase, Lewis Blood Group; Blood group Lewis alpha-4-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
P21217
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Expression Region
Phe30~Lys259
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Molecular Weight
30kDa
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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
FUT3, or fucosyltransferase 3, is an enzyme that plays a critical role in the biosynthesis of fucosylated glycoproteins and glycolipids. Fucosylation is a post-translational modification involving the addition of fucose, a sugar molecule, which can significantly influence cellular processes such as cell adhesion, signaling, and immune responses. The study of FUT3 has garnered attention due to its implications in various physiological and pathological contexts, including developmental biology, cancer progression, and infectious diseases. In particular, altered expression of FUT3 has been associated with enhanced tumor metastasis and altered immune evasion mechanisms in cancer cells. Additionally, FUT3 has been implicated in the modulation of the microbiome and has potential roles in various inflammatory conditions. The recombinant expression of FUT3 provides a valuable tool for investigating its enzymatic activity, substrate specificity, and the biological impacts of fucosylation. Moreover, the development of FUT3 as a therapeutic target is an emerging area of research, presenting opportunities for designing novel interventions that leverage the regulatory roles of fucosylation in human health and disease. Thus, understanding the functional dynamics of FUT3 and its fucosylation processes could lead to significant advancements in the fields of biomedicine and biotechnology.
