THBD Human
Sf9, Baculovirus cells.
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
Greater than 90.0% as determined by SDS-PAGE.
Description
THBD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (22-515a.a) and having a molecular mass of 52.6kDa.
THBD is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
Thrombomodulin (THBD) is a transmembrane glycoprotein primarily found on the surface of endothelial cells. It plays a crucial role in regulating blood coagulation. THBD binds to thrombin, a key enzyme in the coagulation cascade, and this interaction enhances the activation of protein C, an anticoagulant protein. The THBD-thrombin complex promotes the conversion of protein C to its active form, which in turn inhibits excessive clot formation. THBD also influences fibrinolysis, the process of clot breakdown, by activating thrombin-activatable fibrinolysis inhibitor (TAFI). Dysregulation of THBD levels has been implicated in cardiovascular diseases such as atherosclerosis and thrombosis. Additionally, altered THBD levels are associated with conditions like diabetes mellitus, liver cirrhosis, cerebral and myocardial infarction, and multiple sclerosis.
Recombinant human THBD, expressed in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein consists of 500 amino acids (residues 22-515) with an approximate molecular weight of 52.6 kDa. For purification purposes, a 6-amino acid Histidine tag is fused to the C-terminus. The protein is purified using proprietary chromatographic techniques.
The THBD protein is supplied as a solution at a concentration of 0.5 mg/ml. The solution is buffered with Phosphate-Buffered Saline (PBS) at a pH of 7.4 and contains 10% glycerol as a stabilizing agent.
For short-term storage (up to 2-4 weeks), the THBD solution should be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. To prevent protein degradation during long-term storage, adding a carrier protein like HSA or BSA to a final concentration of 0.1% is advised. To maintain protein integrity, it is crucial to avoid repeated freeze-thaw cycles.
The purity of the THBD protein is determined using SDS-PAGE analysis and is consistently greater than 90%.
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
Sf9, Baculovirus cells.
EPQPGGSQCV EHDCFALYPG PATFLNASQI CDGLRGHLMT VRSSVAADVI SLLLNGDGGV GRRRLWIGLQ LPPGCGDPKR LGPLRGFQWV TGDNNTSYSR WARLDLNGAP LCGPLCVAVS AAEATVPSEP IWEEQQCEVK ADGFLCEFHF PATCRPLAVE PGAAAAAVSI TYGTPFAARG ADFQALPVGS SAAVAPLGLQ LMCTAPPGAV QGHWAREAPG AWDCSVENGG CEHACNAIPG
APRCQCPAGA ALQADGRSCT ASATQSCNDL CEHFCVPNPD QPGSYSCMCE TGYRLAADQH RCEDVDDCIL EPSPCPQRCV NTQGGFECHC YPNYDLVDGE CVEPVDPCFR ANCEYQCQPL NQTSYLCVCA EGFAPIPHEP HRCQMFCNQT ACPADCDPNT QASCECPEGY ILDDGFICTD IDECENGGFC SGVCHNLPGT FECICGPDSA LARHIGTDCD SGKVDGGDSG SGEPPPSPTP
GSTLTPPAVG LVHSHHHHHH
Product Science Overview
Thrombomodulin is composed of several domains, each contributing to its function:
- N-terminal domain: Sequesters high-mobility group box 1 (HMGB1), a protein involved in inflammation .
- Epidermal growth factor (EGF)-like domains: These domains are crucial for binding thrombin and activating protein C .
- Serine/threonine-rich domain: This domain is involved in the glycosylation of thrombomodulin, which is essential for its stability and function .
When thrombin binds to thrombomodulin, its procoagulant activity is inhibited, and it promotes the activation of protein C. Activated protein C, in the presence of protein S, inactivates factors Va and VIIIa, thus inhibiting further thrombin generation and clot formation .
Recombinant human thrombomodulin (rhTM), also known as thrombomodulin alfa or ART-123, is a soluble form of thrombomodulin comprising all extracellular domains of the protein . It is developed for therapeutic use, particularly in conditions involving excessive coagulation and inflammation, such as disseminated intravascular coagulation (DIC) and sepsis .
rhTM has shown promise in various clinical settings:
- Thromboembolism and Blood Clotting Disorders: rhTM is investigated for its potential to treat thromboembolism and blood clotting disorders by enhancing the activation of protein C and inhibiting thrombin generation .
- Acute Exacerbation of Idiopathic Pulmonary Fibrosis (IPF): Studies have demonstrated that rhTM treatment can improve the prognosis of patients with acute exacerbation of IPF by reducing inflammation and coagulation .
- Sepsis and Septicemia: rhTM’s anti-inflammatory and anticoagulant properties make it a potential therapeutic agent for sepsis and septicemia .
rhTM enhances the activation of pro-carboxypeptidase B2 (pro-CPB2) by thrombin. Activated pro-CPB2 (CPB2) exerts anti-inflammatory and anti-fibrinolytic activities . By binding to thrombin, rhTM inhibits its procoagulant activity and promotes the activation of protein C, which in turn inactivates factor Va in the presence of protein S . This mechanism helps to attenuate the extension of clots while other anticoagulants inhibit the initiation of clot formation .
