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murine Mab against human Thrombomodulin
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murine Mab against human Thrombomodulin
Thrombomodulin (TM) is the cell surface receptor for thrombin. When occupied, thrombomodulin converts thrombin from a procoagulant protein into the activator of Protein C. 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, 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.
No. 2375 reacts with the EGF1 EGF2 region of thrombomodulin. No cross reactivity observed with other known human coagulation proteins at 10 fold excess concentration.
Size: 250 µg
Source: Mouse
Clonality: AD-1 / 71-43B
Storage temperature: 2-8C
Transport temperature: Room temperature
Delivery time: 2-14days
Supplier: ImmBioMed/LOXO GmbH
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, 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.
No. 2375 reacts with the EGF1 EGF2 region of thrombomodulin. No cross reactivity observed with other known human coagulation proteins at 10 fold excess concentration.
Size: 250 µg
Source: Mouse
Clonality: AD-1 / 71-43B
Storage temperature: 2-8C
Transport temperature: Room temperature
Delivery time: 2-14days
Supplier: ImmBioMed/LOXO GmbH
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