Analytical Data
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Gene name
TFPI
- Application
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Alternative Names
TFPI；LACI；TFPI1；Tissue factor pathway inhibitor
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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
P10646-2
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Expression Region
152-251aa
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AA Sequence
RFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQ STKVPSLFVTKEGTNDGWKSAAHIYQVFLNAFCIHASMFFLGLDSISCLC
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Molecular Weight
37 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
Related Products
Protein Description
Tissue Factor Pathway Inhibitor (TFPI) is a critical protein that regulates hemostasis by inhibiting the extrinsic pathway of coagulation. Its primary function is to bind to the tissue factor-factor VIIa complex, thereby preventing the activation of factor X and ultimately inhibiting thrombin generation. The importance of TFPI in maintaining the balance between coagulation and fibrinolysis has made it a focal point of research, particularly in the context of thrombotic disorders and cardiovascular diseases. Studies have shown that altered levels of TFPI can contribute to various pathological conditions, including venous thromboembolism and atherosclerosis. Additionally, TFPI has been implicated in cancer biology, where tumor cells may exploit coagulation pathways for growth and metastasis. The production of recombinant TFPI proteins has provided a valuable tool for both therapeutic and research applications, allowing for the examination of its biological functions and potential as a therapeutic agent. Given the complexities of coagulation pathways and the role of TFPI as a natural inhibitor, ongoing research aims to elucidate its mechanisms of action and explore its possibilities in clinical applications, including the development of novel anticoagulant therapies. This area of study holds promise for improving outcomes in patients at risk for thrombotic events, making TFPI an important target in the fields of hematology and cardiology.
