Bovine Thrombin Recombinant Protein (RPPB5147)
- SKU:
- RPPB5147
- Product Type:
- Recombinant Protein
- Species:
- Bovine
Description
| Product Name: | Bovine Thrombin Recombinant Protein |
| Product Code: | RPPB5147 |
| Size: | 10000U |
| Species: | Bovine |
| Target: | Thrombin |
| Synonyms: | Coagulation Factor II (Thrombin), Prepro-Coagulation Factor II, EC 3.4.21.5, RPRGL2, THPH1, Coagulation Factor II, Prothrombin B-Chain, Serine Protease, Prothrombin, EC 3.4.21, PT, F2. |
| Source: | Bovine Blood |
| Physical Appearance: | Sterile Filtered light brown�lyophilized (freeze-dried) powder. |
| Formulation: | Lyophilized freeze dry powder formulated with Tris buffer, HCl and sodium chloride, PH 7.5. |
| Solubility: | It is recommended to reconstitute the lyophilized Thrombin in sterile 18M?-cm H2O. |
| Stability: | Lyophilized Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution�Thrmbin should be stored at 4°C between 2-7 days and for future use below -18°C.�For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles. |
| Biological Activity: | Activity was determined by the direct comparison to NIH Thrombin Reference Standard which uses 200ul of diluted plasma 1:1 with saline as a substrate and 100ul of albumin solution based on a modification of the method of Biggs. The clotting durations for determining thrombin activity are in the range of 15�25 seconds at 37C. The specific activity found was 176 NIH units per mg. |
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
