Analytical Data
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Gene name
FUT2
- Application
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Alternative Names
SE; Se2; Sej; Secretor Status Included; Galactoside 2-Alpha-L-Fucosyltransferase 2; Secretor blood group alpha-2-fucosyltransferase; Secretor factor
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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
Q10981
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Expression Region
Gln29~His343
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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
Related Products
Protein Description
FUT2 (fucosyltransferase 2) is an important enzyme involved in the fucosylation of glycoproteins and glycolipids, a post-translational modification that plays a critical role in various biological processes, including cell signaling, immune response, and pathogen recognition. The gene encoding FUT2 is polymorphic, with certain alleles influencing the expression of fucosylated antigens on the surface of epithelial cells, particularly in the human gastrointestinal tract. Research has shown that individuals with specific FUT2 variants, such as the non-secretor phenotype, exhibit altered susceptibility to infections, including those caused by pathogens like norovirus. As a result, the study of FUT2 recombinant proteins has gained traction, as these proteins could facilitate a better understanding of the enzyme's functionality, its role in glycan biosynthesis, and its potential therapeutic applications. Utilizing recombinant DNA technology to express and purify FUT2 proteins allows for in-depth characterization of their kinetic properties, substrate specificity, and regulatory mechanisms. Furthermore, investigating the interaction between FUT2 and its metabolites could unveil new pathways and mechanisms influencing human health and disease, potentially leading to novel biomarker development and targeted therapeutic strategies against infections and inflammatory conditions. Overall, the exploration of FUT2 recombinant proteins is not only significant for advancing the field of glycobiology but also holds promise for clinical implications in understanding disease susceptibility and developing personalized medicine approaches.
