605190-M
Thrombin, Human Plasma
Synonym(s):
Thrombin, Human Plasma
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biological source
human plasma
Quality Level
description
Merck USA index - 14, 9383
form
lyophilized
specific activity
≥1000 NIH units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
solubility
water: 1 mg/mL
aqueous buffer: soluble
storage temp.
−20°C
General description
Application
Thrombin, Human Plasma has been used:
- as a component of endothelial growth medium (EGM) media for the transplantation and reisolation of Kaposi′s sarcoma-associated herpesvirus-human endothelial cell line (KSHV-HuARLT) cells from mice[3]
- for the fabrication of fibrin gels[4]
- as a component of EGM media for viral copy number analysis of KSHV-HuARLT cells and matrigel implant[5]
Biochem/physiol Actions
Physical form
Lyophilized from 200 mM NaCl, 50 mM citrate buffer, 0.1% PEG-8000, pH 6.5. Contains BSA as a stabilizer.
Preparation Note
Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 2 months at -70°C.
Prepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Analysis Note
Complete activation from homogeneous prothrombin by SDS-PAGE
Other Notes
One unit is determined by comparison with a standard curve prepared using the Bureau of Biologics standard thrombin.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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.
Toxicity: Harmful (C)
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Segall JA and Liem TK
Congenital and Acquired Hypercoagulable Syndromes, 339-346 (2007)
Kitchens CS, et al
Consultative Hemostasis and Thrombosis (2013)
Diana L Diesen et al.
Vascular, 16 Suppl 1, S29-S36 (2008-03-01)
Thrombin is a common hemostatic drug used in surgical practice for over 100 years because of its simplicity and efficacy. Thrombin converts fibrinogen to fibrin, activates platelets, and induces vascular contraction. It is available in multiple forms, including human thrombin
Isis S R Carter et al.
Thrombosis, 2010, 416167-416167 (2010-01-01)
Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region
Madhavi A Jadhav et al.
Biochemistry, 49(13), 2918-2924 (2010-03-12)
The formation of a blood clot involves the interplay of thrombin, fibrinogen, and Factor XIII. Thrombin cleaves fibrinopeptides A and B from the N-termini of the fibrinogen Aalpha and Bbeta chains. Fibrin monomers are generated that then polymerize into a
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