T4393
Thrombin from human plasma
lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture
Synonym(s):
Factor IIa
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About This Item
CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.75
EC Number:
232-648-7
MDL number:
Product Name
Thrombin from human plasma, lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture
biological source
human plasma
sterility
sterile
form
lyophilized powder
specific activity
1500-3500 NIH units/mg protein (E1%/280, 18.3)
technique(s)
cell culture | mammalian: suitable
impurities
HIV, hepatitis B and hepatitis C, tested negative
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
human ... F2(2147)
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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.
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).
Other Notes
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard
Preparation Note
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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A small trypsin inhibitor from the frog of Odorrana grahami
Li J, et al.
Biochimie, 90(9), 1356-1361 (2008)
Thrombin action on astrocytes in the hindbrain of the rat disrupts glycemic and respiratory control.
Richard C Rogers et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 318(6), R1068-R1077 (2020-04-23)
Severe trauma can produce a postinjury "metabolic self-destruction" characterized by catabolic metabolism and hyperglycemia. The severity of the hyperglycemia is highly correlated with posttrauma morbidity and mortality. Although no mechanism has been posited to connect severe trauma with a loss
Thrombin generation correlates with disease duration in multiple sclerosis (MS): Novel insights into the MS-associated prothrombotic state
Parsons MEM, et al.
Multiple Sclerosis Journal, 3(4) (2017)
Endothelial cell processing and alternatively spliced transcripts of factor VIII: potential implications for coagulation cascades and pulmonary hypertension
Shovlin CL, et al.
PLoS ONE, 5(2), e9154-e9154 (2010)
Thrombin and prothrombin are expressed by neurons and glial cells and accumulate in neurofibrillary tangles in Alzheimer disease brain
Arai T, et al.
Journal of Neuropathology and Experimental Neurology, 65(1), 19-25 (2006)
Articles
Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.
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