Analytical Data
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Gene name
TFPI2
- Application
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Alternative Names
TFPI2；Tissue factor pathway inhibitor 2
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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
P48307
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Expression Region
23-213aa
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AA Sequence
DAAQEPTG NNAEICLLPL DYGPCRALLL RYYYDRYTQS CRQFLYGGCE GNANNFYTWE ACDDACWRIE KVPKVCRLQV SVDDQCEGST EKYFFNLSSM TCEKFFSGGC HRNRIENRFP DEATCMGFCA PKKIPSFCYS PKDEGLCSAN VTRYYFNPRY RTCDAFTYTG CGGNDNNFVS REDCKRACAK ALK
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Molecular Weight
23 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
TFPI2, or Tissue Factor Pathway Inhibitor 2, is a serine protease inhibitor that plays a critical role in regulating coagulation and maintaining hemostatic balance. It primarily inhibits the tissue factor (TF)-FVIIa complex, which is essential for initiating the extrinsic pathway of blood coagulation. Research has shown that alterations in TFPI2 expression are associated with various pathological conditions, including cancer, cardiovascular diseases, and inflammatory disorders. Given its pivotal role in vascular homeostasis and thrombosis, TFPI2 has garnered attention as a potential therapeutic target. Recombinant TFPI2 proteins are being studied for their potential applications in anticoagulation therapy, as well as for their ability to modulate tumor microenvironments and improve outcomes in cancer treatments. Furthermore, detailed characterization of TFPI2’s structure and function can provide insights into its regulatory mechanisms, enhancing the understanding of coagulation processes and leading to novel treatment strategies. As such, the investigation of TFPI2 recombinant proteins not only furthers our knowledge of hemostatic regulation but also holds promise for innovative therapeutic interventions in various diseases.
