Thrombin from human plasma
SIGMA/T1063 - lyophilized powder, ≥2800 NIH units/mg protein (E1%/280 , 18.3)
Synonym: Factor IIa
CAS Number: 9002-04-4
EC Number: 232-648-7
MDL Number: MFCD00082072
Product Type: Chemical
Prothrombin is cleaved in vivo by activated factor X releasing the activation peptide and cleaving thrombin into light and heavy chains yielding catalytically active α-thrombin. α-Thrombin is composed of a light chain (A chain)(MW ~6,000) and a heavy chain (B chain)(~31,000). These two chains are joined by one disulfide bond.
| application(s) | diagnostic assay manufacturing |
| form | lyophilized powder |
| impurities | HIV, hepatitis B and hepatitis C, tested negative |
| mol wt | 37.4 kDa |
| Quality Level | 200  |
| specific activity | ≥2800 NIH units/mg protein (E |
| storage temp. | −20°C |
| UniProt accession no. | P00734  |
| Analysis Note: | The NIH assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations. |
| Application: | Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to evaluate the in vitro effect of low molecular weight heparin on thrombin generation in cirrhotic patients at different stages of liver disease. |
| Biochem/physiol Actions: | Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B. |
| Disclaimer: | RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization. |
| General description: | Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. |
| Other Notes: | Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard |
| Other Notes: | View more information on thrombin at www.sigma-aldrich.com/enz. |
| Physical form: | Lyophilized from 0.02 M Bis/Tris buffer, pH 6.5, 0.15 M NaCl and 0.1% PEG-8000 |
| Symbol |   GHS07,GHS08 |
| Signal word | Danger |
| Hazard statements | H315 - H319 - H334 - H335 |
| Precautionary statements | P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 |
| Hazard Codes | Xn |
| Risk Statements | 36/37/38-42 |
| Safety Statements | 22-24-26-36/37 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 2 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥2800 NIH units/mg protein (E |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.21.5 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |