Recombinant Proteins

p53
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TFPI Human

Tissue Factor Pathway Inhibitor Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT13564
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

TFPI Human, Sf9

Tissue Factor Pathway Inhibitor Human Recombinant, Sf9

TFPI Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 285 amino acids (29-304a.a.) and having a molecular mass of 33kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TFPI is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT13647
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

TFPI2 Human

Tissue Factor Pathway Inhibitor 2 Human Recombinant

TFPI2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 199 amino acids (23-213 a.a.) and having a molecular mass of 22.9kDa (Migrates at 18-40kDa on SDS-PAGE under reducing conditions).
TFPI2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13742
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.
Definition and Classification

Tissue Factor Pathway Inhibitor (TFPI) is a protease inhibitor that plays a crucial role in regulating the tissue factor (TF)-initiated blood coagulation cascade. It is a single-chain polypeptide that can reversibly inhibit factor Xa (FXa) and subsequently inhibit the FVIIa-TF complex . TFPI is classified into two main isoforms: TFPIα and TFPIβ .

Biological Properties

Key Biological Properties: TFPI is a multivalent Kunitz-type proteinase inhibitor with three tandem Kunitz-type inhibitor domains . TFPIα has three Kunitz domains (K1, K2, K3) and a basic C terminus, while TFPIβ has K1 and K2 domains attached to a glycosylphosphatidyl inositol-anchored C terminus .

Expression Patterns: TFPIα is the only isoform present in platelets, whereas endothelial cells produce both isoforms, secreting TFPIα and expressing TFPIβ on the cell surface .

Tissue Distribution: TFPI is expressed in various tissues, including the liver, lungs, and placenta . It is also found in endothelial cells and platelets .

Biological Functions

Primary Biological Functions: TFPI is the primary inhibitor of the initiation of blood coagulation. It inhibits the TF-FVIIa complex and FXa, thereby modulating the severity of bleeding and clotting disorders .

Role in Immune Responses and Pathogen Recognition: TFPI also plays a role in immune responses by inhibiting TF-dependent cellular signaling, which can influence inflammatory and cancer pathologies .

Modes of Action

Mechanisms with Other Molecules and Cells: TFPI inhibits the TF-FVIIa complex and FXa through high-affinity interactions. Protein S enhances FXa inhibition by TFPIα .

Binding Partners: TFPI binds to TF, FVIIa, and FXa to form inhibitory complexes .

Downstream Signaling Cascades: TFPI suppresses TF-dependent cellular signaling, which can influence various cellular processes, including inflammation and cancer progression .

Regulatory Mechanisms

Regulatory Mechanisms: TFPI expression and activity are regulated through transcriptional and post-translational modifications. An alternative splicing event in the 5′ untranslated region allows for translational regulation of TFPIβ expression .

Transcriptional Regulation: TFPI gene expression is regulated by various transcription factors and signaling pathways .

Post-Translational Modifications: TFPI undergoes post-translational modifications, including glycosylation, which can influence its activity and stability .

Applications

Biomedical Research: TFPI is used in research to study coagulation disorders and the development of anticoagulant therapies .

Diagnostic Tools: TFPI levels can be measured to diagnose and monitor bleeding and clotting disorders .

Therapeutic Strategies: TFPI and its analogs are being explored as potential therapeutic agents for treating coagulation disorders and certain cancers .

Role in the Life Cycle

Role Throughout the Life Cycle: TFPI plays a critical role in regulating blood coagulation throughout the life cycle. It is essential for embryonic development, particularly in the central nervous system . TFPI also influences vascular development, cellular migration, and tumor angiogenesis .

From Development to Aging and Disease: TFPI’s regulatory functions are crucial from embryogenesis to aging. Dysregulation of TFPI activity can lead to various pathological conditions, including thrombosis, hemorrhage, and cancer .

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