Analytical Data
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Gene name
FUT8
- Application
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Alternative Names
FUT8；Alpha-(1.6)-fucosyltransferase
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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
Q9BYC5
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Expression Region
1-575aa
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AA Sequence
MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDHPDHSSRELSKILAKL ERLKQQNEDLRRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENY KKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNELQRHAD EFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQN PKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRY ATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPR PPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEAT KKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVD KKRVYLATDDPSLLKEAKTKYPNYEFISDNSISWSAGLHNRYTENSLRGV ILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFHSLDDIYYFG GQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYSKGVNRKLGRT GLYPSYKVREKIETVKYPTYPEAEK
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Molecular Weight
89 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
The FUT8 recombinant protein has garnered significant interest in the fields of glycobiology and therapeutic development due to its pivotal role in glycosylation, specifically in the fucosylation of glycoproteins. Fucosylation is an essential post-translational modification that influences protein stability, immune recognition, and cell signaling, making it crucial for various biological processes and disease mechanisms. Aberrant fucosylation is associated with several pathological conditions, including cancer, inflammatory diseases, and infectious diseases, highlighting the importance of understanding FUT8's function. As a key enzyme, FUT8 catalyzes the addition of fucose residues to specific glycan structures, which can alter cell behavior and messaging within the immune system. Current research aims to elucidate the structural and functional characteristics of FUT8, employing recombinant expression systems to produce functional FUT8 proteins for biochemical and biophysical studies. These investigations are critical for delineating the enzyme's mechanism of action, its role in health and disease, and its potential as a therapeutic target. Furthermore, the recombinant FUT8 protein may facilitate the development of novel glyco-engineered biopharmaceuticals, enabling enhanced efficacy and reduced immunogenicity due to optimized glycosylation patterns. As such, FUT8 represents a promising area of study within glycoengineering and personalized medicine, with the potential to unlock new avenues for disease intervention and treatment.
