Analytical Data
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Gene name
POFUT1
- Application
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Alternative Names
POFUT1;FUT12;KIAA0180;GDP-fucose Protein O-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
Q9H488
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Expression Region
27-388aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF
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Molecular Weight
44 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
POFUT1, or Protein O-Fucosyltransferase 1, is an essential enzyme involved in the modification of Notch receptors through the addition of fucose residues. This glycosylation process plays a critical role in the proper functioning of Notch signaling pathways, which are crucial for various biological processes, including cell differentiation, proliferation, and apoptosis. Dysregulation of Notch signaling has been implicated in numerous diseases, including cancer and developmental disorders. Therefore, understanding the structure and function of POFUT1 is vital for elucidating its role in these pathways and its potential as a therapeutic target. Recent studies have focused on the recombinant expression of POFUT1 to investigate its enzyme kinetics, substrate specificity, and interaction with other proteins in the signaling pathways. The ability to produce POFUT1 in a controlled laboratory setting allows researchers to explore its enzymatic activity and functional implications in greater detail, paving the way for potential interventions in diseases associated with Notch signaling dysregulation. As the demand for targeted therapies grows, the characterization of POFUT1 as a functional protein holds promise for advancing our understanding of glycosylation processes and their impact on human health.
