605190-M
Thrombin, Human Plasma
Sinônimo(s):
Thrombin, Human Plasma
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About This Item
Produtos recomendados
fonte biológica
human plasma
Nível de qualidade
forma
lyophilized
atividade específica
≥1000 NIH units/mg protein
fabricante/nome comercial
Calbiochem®
condição de armazenamento
OK to freeze
solubilidade
water: 1 mg/mL
aqueous buffer: soluble
temperatura de armazenamento
−20°C
Descrição geral
Thrombin, a sodium-activated type II enzyme, comprises two anion binding exosites, ABE-I and ABE-II. This serine protease enzyme is synthesized from zymogen prothrombin (factor II) in the liver.
Aplicação
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
- for the fabrication of fibrin gels
- as a component of EGM media for viral copy number analysis of KSHV-HuARLT cells and matrigel implant
Ações bioquímicas/fisiológicas
Thrombin cleaves and converts fibrinogen into fibrin. It then activates factors V, VIII, XI, and XIII. Thrombin stimulates platelet activation and stabilizes the fibrin polymers. It elicits a vital role in the last stages of the blood coagulation cascade.
Advertência
Toxicity: Harmful (C)
Definição da unidade
One unit is determined by comparison with a standard curve prepared using the Bureau of Biologics standard thrombin.
forma física
Lyophilized from 200 mM NaCl, 50 mM citrate buffer, 0.1% PEG-8000, pH 6.5. Contains BSA as a stabilizer.
Nota de preparo
Prepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstituição
Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 2 months at -70°C.
Nota de análise
Complete activation from homogeneous prothrombin by SDS-PAGE
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Exoneração de responsabilidade
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.
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órgãos-alvo
Respiratory system
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (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
Dillon K Jarrell et al.
PloS one, 16(5), e0239242-e0239242 (2021-05-20)
Fibrin has been used clinically for wound coverings, surgical glues, and cell delivery because of its affordability, cytocompatibility, and ability to modulate angiogenesis and inflammation. However, its rapid degradation rate has limited its usefulness as a scaffold for 3D cell
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