TFPI Human

Tissue Factor Pathway Inhibitor Human Recombinant
Cat. No.
BT13564
Source
Escherichia Coli.
Synonyms
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

TFPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (29-304) and having a molecular mass of 34.3kDa.
TFPI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tissue Factor Pathway Inhibitor (TFPI) is a key regulator of the coagulation cascade, specifically targeting the extrinsic pathway. This pathway is initiated upon tissue factor (TF) exposure, leading to the formation of the TF-VIIa complex. This complex subsequently activates factors IX and X, ultimately culminating in fibrin clot formation. TFPI exerts its inhibitory action by binding to and inactivating both factor Xa and the TF-VIIa complex, thereby playing a crucial role in the negative feedback regulation of coagulation. Synthesized primarily in the vascular endothelium, TFPI exists in both free and lipoprotein-bound forms within the circulation. While several alternatively spliced TFPI transcripts have been identified, the complete structure of some remains to be fully elucidated.
Description
Recombinant Human TFPI, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 299 amino acids (residues 29-304). The protein, with a molecular weight of 34.3 kDa, incorporates a 23-amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The TFPI solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. The addition of a carrier protein such as HSA or BSA (0.1%) is advised for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity is determined to be greater than 85.0% as assessed by SDS-PAGE analysis.
Synonyms
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNM.

Product Science Overview

Introduction

Tissue Factor Pathway Inhibitor (TFPI) is a crucial protein in the regulation of blood coagulation. It is a Kunitz-type serine protease inhibitor that plays a significant role in inhibiting the tissue factor (TF)-initiated blood coagulation pathway. The recombinant form of TFPI, known as Human Recombinant TFPI, is produced using recombinant DNA technology, allowing for its use in various therapeutic and research applications.

Structure and Function

TFPI is composed of three tandem Kunitz-type inhibitor domains. Each domain has a specific function in the inhibition process:

  1. First Kunitz Domain: This domain inhibits the factor VIIa (FVIIa) and tissue factor (TF) complex.
  2. Second Kunitz Domain: This domain inhibits factor Xa (FXa).
  3. Third Kunitz Domain: Although it does not inhibit protease activity, it plays a crucial role in the overall function of TFPI .

The primary function of TFPI is to inhibit the TF-initiated blood coagulation cascade. It achieves this by forming a complex with FVIIa/TF via the first Kunitz domain and with FXa via the second Kunitz domain. This dual inhibition mechanism is essential for maintaining hemostasis and preventing excessive blood clotting .

Genetic and Molecular Background

The gene encoding TFPI is located on chromosome 2q31-q32.1 and consists of nine exons spanning approximately 70 kilobases. TFPI is expressed in various tissues, including endothelial cells, megakaryocytes, and liver cells . The protein has a molecular weight of approximately 34,000 to 40,000 Daltons, depending on the degree of proteolysis of the C-terminal region .

Clinical Significance

TFPI plays a vital role in regulating blood coagulation and maintaining vascular integrity. Its deficiency or dysfunction can lead to thrombotic disorders, where excessive blood clotting occurs. Conversely, elevated levels of TFPI have been associated with bleeding disorders .

Recombinant TFPI has therapeutic potential in treating conditions related to abnormal blood coagulation. It is being investigated for its use in managing sepsis, where uncontrolled coagulation and inflammation occur, and in treating thrombotic disorders .

Research and Therapeutic Applications

Human Recombinant TFPI is used in various research and clinical applications. It is utilized to study the mechanisms of blood coagulation and to develop new therapeutic strategies for managing coagulation disorders. Additionally, recombinant TFPI is being explored for its potential in treating cardiovascular diseases and cancer, where abnormal coagulation and angiogenesis play a role .

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