Analytical Data
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Gene name
FUT3
- Application
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Alternative Names
FUT3；FT3B；LE；PCSK3;3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
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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
P21217
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Expression Region
35-361aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT
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Molecular Weight
41 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
FUT3, or fucosyltransferase 3, is an enzyme that plays a critical role in the process of fucosylation, which involves the addition of fucose, a type of sugar, to glycoproteins and glycolipids. This modification significantly influences various biological processes, including cell-cell interactions, immune responses, and tumor progression. Recent studies have highlighted the importance of FUT3 in mediating the adhesion of cancer cells to the vascular endothelium, which is a crucial step in metastasis. Given its pivotal role in tumor biology and immune regulation, FUT3 has emerged as a potential therapeutic target for cancer treatment. The study of recombinant FUT3 proteins enables researchers to explore its enzymatic activity, substrate specificity, and the effects of fucosylation on cellular functions. Advances in recombinant protein technology have facilitated the production of pure FUT3, allowing for detailed functional assays and structural analyses. This research not only enhances our understanding of FUT3's biological significance but also paves the way for the development of FUT3 inhibitors that could serve as novel anticancer agents. By elucidating the mechanisms by which FUT3 contributes to disease progression, scientists aim to identify potential biomarkers for cancer diagnostics and prognosis, ultimately improving patient outcomes through targeted therapeutic strategies.
