Analytical Data
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基因名
TFPI
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简介
TFPI protein, encoded by the TFPI gene, is an important Kunitz-type serine protease inhibitor that regulates TF-dependent pathways in coagulation. It inhibits factor X and VIIa-TF proteases, preventing excessive clot formation. TFPI Protein, Human (HEK293, His) is the recombinant human-derived TFPI protein, expressed by HEK293 , with C-6*His labeled tag.
- Application
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别名
Tissue factor pathway inhibitor; EPI; LACI; TFPI1
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种属
Human
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表达系统
HEK293
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P10646
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表达区间
D29-K282
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氨基酸序列
DSEEDEEHTIITDTELPPLKLMHSFCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNQNRFESLEECKKMCTRDNANRIIKTTLQQEKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQSTKVPSLFEFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGCGGNENNFTSKQECLRACKKGFIQRISKGGLIK
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蛋白长度
Partial
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分子量
42-45 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
Tissue factor pathway inhibitor (TFPI) is a critical regulator of the coagulation cascade, playing a vital role in maintaining hemostasis and preventing thrombosis. Discovered in the 1980s, TFPI acts primarily by inhibiting factor Xa and tissue factor (TF), thereby controlling the formation of the thrombin complex necessary for blood clotting. Given its central role in coagulation, researchers have focused on developing recombinant forms of TFPI for therapeutic applications. These recombinant proteins have potential use in treating various thromboembolic disorders, including deep vein thrombosis and pulmonary embolism, as well as in preventing clot formation in patients undergoing certain surgical procedures. The production of recombinant TFPI presents challenges, including ensuring proper folding, post-translational modifications, and bioactivity. Advances in biotechnology, such as genetic engineering techniques, have enabled the successful expression of TFPI in different host systems, including bacteria and mammalian cells. Recent studies have highlighted the efficacy of recombinant TFPI in preclinical models, demonstrating its ability to modulate coagulation pathways effectively. This progress paves the way for clinical trials aimed at evaluating its safety and efficacy, potentially offering new therapeutic avenues for patients at risk of thrombotic events. Overall, the research on TFPI recombinant proteins holds promise for enhancing our understanding of coagulation biology and developing targeted treatments for thrombotic diseases.
