Analytical Data
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基因名
POFUT1
- Application
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别名
POFUT1;FUT12;KIAA0180;GDP-fucose Protein O-fucosyltransferase 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9H488
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表达区间
27-388aa
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氨基酸序列
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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分子量
44 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
