Analytical Data
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Gene name
FUT5
- Application
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Alternative Names
FUT5；4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5
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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
Q11128
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Expression Region
1-374aa
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AA Sequence
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPNGSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVIVHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFHWRETLRPRSFSWALAFCKACWKLQQESRYQTVRSIAAWFT
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Molecular Weight
42.9 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
FUT5, or fucosyltransferase 5, is an important enzyme involved in the biosynthesis of fucosylated glycans, which play crucial roles in cell-cell interactions, immune responses, and various biological processes. Research on FUT5 has gained prominence due to its association with several pathophysiological conditions, including cancer, viral infections, and inflammatory diseases. Fucosylation is a post-translational modification that adds fucose, a type of sugar, to proteins and lipids, influencing their stability and interactions. Specifically, FUT5 catalyzes the addition of fucose to specific glycan structures, which can modulate receptor-ligand binding, enhance pathogenicity in viral infections, and alter immune cell signaling. Understanding FUT5 and its mechanism can provide insights into therapeutic strategies aimed at manipulating fucosylation patterns for cancer treatment, vaccine development, and enhancing immune responses. Recent advancements in recombinant protein technology have facilitated the expression and purification of FUT5, enabling detailed studies of its enzymatic activity, substrate specificity, and structural characteristics. Consequently, the exploration of FUT5's role in various biological contexts has the potential to unveil novel biomarkers for disease and new targets for drug development, making it a significant focus of current glycobiology research.
