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Thrombin from human plasma

SIGMA/T4393 - lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture

Synonym: Factor IIa

CAS Number: 9002-04-4
EC Number: 232-648-7
MDL Number: MFCD00082072
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-T4393-100UN 100 units
$308.00
1/EA
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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.

 

biological source human plasma
form lyophilized powder
impurities HIV, hepatitis B and hepatitis C, tested negative
Quality Level 200 
specific activity 1500-3500 NIH units/mg protein (E1%/280, 18.3)
sterility sterile
storage temp. −20°C
technique(s) cell culture | mammalian: suitable
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 from human plasma has been used:
• as a medium supplement for the pre-treatment of endothelial cell culture prior to confocal microscopy and enzyme linked immunosorbent assay (ELISA)
• in the gelatinization of mesenchymal stem cells (MSCs) for preparing fibrin–MSC construct
• for screening serine protease inhibitor, OGTI from frog skin secretion

Biochem/physiol Actions: Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
Biochem/physiol Actions: The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation. High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease. A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia. Altered thrombin levels modulates the coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin. Thrombin accumulation in neurofibrillary tangles in the brain may contribute to the aggregation of τ protein and pathophysiology of Alzheimer disease.
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 produced from the proteolytic cleavage of inactive prothrombin in the liver. The prothrombin gene is mapped to human chromosome 11p11.2. It comprises of A and B catalytic domain, recognition domain and insertion loops. The active site residues comprise the catalytic tetrad, (histidine 57, aspartate 102, serine 195 and serine 214).
Reconstitution: When reconstituted with 1 mL water, vial contains stated activity in 0.15 M sodium chloride and 0.05 M sodium citrate, pH 6.5.
Unit Definition: Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard
Symbol GHS08  GHS08
Signal word Danger
Hazard statements H334
Precautionary statements P261 - P284 - P501
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 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
activity specific activity: 1500-3500 NIH units/mg protein (E1%/280, 18.3)
Storage Temp. −20°C
Enzyme Commission (EC) Number 3.4.21.5   ( BRENDA  | IUBMB  )
UNSPSC 12352202

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