Thrombomodulin, human 人血栓調節蛋白

cat#2374

Description

Thrombomodulin (TM) is the cell surface receptor for thrombin. When occupied, thrombomodulin converts thrombin from a procoagulant protein into the activator of Protein C.1,2 After activating Protein C, thrombomodulin acts as a major anticoagulant through its ability to inactivate various blood factors (Va, VIIIa, Xa and XIIIa). In competing for thrombin binding, thrombomodulin inhibits the proteolytic effect of thrombin in its clotting of fibrinogen, the inactivation of Protein S and the induction of platelet aggregation.

TM is similar in structure to the low-density lipoprotein (LDL) receptor. TM possesses several EGF repeats, of which numbers five and six are responsible for the high affinity binding of thrombin (Kd = 0.5 nM). In addition, the B chain of thrombin possesses a domain, distinct from the active catalytic site, termed anion-binding Exosite I, which is involved in the binding of thrombin to thrombomodulin. TM contains a chondroitin sulfate (glycosoaminoglycan) which accelerates the inactivation of thrombin by anti-thrombin III. On SDS-polyacrylamide gels, native human thrombomodulin appears as a single band at Mr 75,000 D under non-reducing conditions and shows a band at approximately Mr 110,000 D following reduction of its disulfide bonds.

The thrombomodulin-thrombin complex enhances the catalytic activation of Protein C over 1,000 fold3. The binding of thrombin to thrombomodulin does not require calcium; however, interaction of the complex with Protein C is calcium dependent. Platelets, monocytes and neutrophils contain small amounts of TM in comparison to cultured endothelial cells. Immunohistochemical analysis has localized TM to the luminal surface of endothelium of blood vessels and lymphatics, the squamous epithelium, and the placental syncytiotrophoblast.

REF 2374 is a recombinant carboxy-terminal truncated form of thrombomodulin and lacks the putative transmembrane and cytoplasmic domains, approximately 38 amino acids.

Preparation

REF 2374 has been expressed by a mammalian cell line and purified by reverse phase, ion exchange and size-exclusion chromatography. Purity is determined via SDS-PAGE analysis. Under reducing conditions, the protein migrates as a single band at 51,000 Da.

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