Analytical Data
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Gene name
FUT1
- Application
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Alternative Names
FUT1；H；HSC；Galactoside alpha-(1.2)-fucosyltransferase 1
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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
P19526
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Expression Region
1-365aa
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AA Sequence
MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGTAMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAALAPVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQIRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSAYLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLWTLAKP
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Molecular Weight
41.2 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
FUT1, or fucosyltransferase 1, is a crucial enzyme involved in the fucosylation of glycoconjugates, a process that adds fucose, a type of sugar, to proteins and lipids. This modification plays a significant role in various biological processes, including cell signaling, immune response, and pathogen interaction. Abnormalities in fucosylation have been implicated in several diseases, including cancer, where altered FUT1 expression can affect tumor progression and metastasis. Research on FUT1 has garnered attention due to its potential as a therapeutic target; understanding its regulatory mechanisms could lead to novel treatments for diseases associated with altered fucosylation. Furthermore, FUT1's role in the formation of blood group antigens highlights its importance in transfusion medicine and organ transplantation. Recent advances in molecular biology techniques have enabled researchers to explore the structural and functional aspects of FUT1, as well as its interaction with other glycosyltransferases and substrates. Investigating the expression patterns of FUT1 in different tissues and conditions also provides valuable insights into its physiological and pathological roles, making it a significant focus of current glycoscience research.
