Analytical Data
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Gene name
FUT8
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简介
The FUT8 protein acts as a catalyst during glycosylation, specifically adding fucose in an α1-6 linkage to the first GlcNAc residue located near the N-glycan peptide chain. This enzymatic activity plays a crucial role in glycoprotein modification, contributing to the structural diversity and functional properties of N-glycans. FUT8 Protein, Human (sf9, His) is the recombinant human-derived FUT8 protein, expressed by Sf9 insect cells , with C-His labeled tag.
- Application
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Alternative Names
Alpha-(1,6)-fucosyltransferase; Alpha1-6FucT; FUT8; Fucosyltransferase 8
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Species
Human
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Source
Baculovirus
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BYC5-1
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Expression Region
R68-K575
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Protein Length
Partial
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Molecular Weight
55 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
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Protein Description
FUT8 (Fucosyltransferase 8) is an important glycosyltransferase enzyme that catalyzes the fucosylation of glycoproteins, which is a critical post-translational modification influencing various biological processes, including cell adhesion, migration, and immune response. The study of FUT8 has gained attention due to its potential implications in cancer biology, where altered fucosylation patterns have been associated with tumor progression and metastasis. Additionally, FUT8 plays a significant role in the regulation of glycan structures on cell surface proteins, which can affect receptor-ligand interactions and signal transduction pathways. Understanding the enzymatic mechanism of FUT8 and its substrate specificity is crucial for deciphering its biological functions and potential therapeutic applications. Research has focused on the recombinant production of FUT8 to facilitate enzyme characterization, study its role in various diseases, and explore its potential as a target for novel anti-cancer therapies. By elucidating the structure-function relationship of FUT8, researchers aim to develop inhibitors that could modulate its activity, thereby offering new avenues for cancer treatment and diagnosis. The ongoing investigation into FUT8 not only enhances our knowledge of glycosylation but also contributes to the broader field of glycobiology, which is fundamental for the development of glyco-engineered therapeutics.
