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605190-M

Sigma-Aldrich

Thrombin, Human Plasma

Synonym(s):

Thrombin, Human Plasma

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About This Item

CAS Number:
9002-04-4
UNSPSC Code:
12352202
NACRES:
NA.51

biological source

human plasma

Quality Level

100

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

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.

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
  • for the fabrication of fibrin gels
  • as a component of EGM media for viral copy number analysis of KSHV-HuARLT cells and matrigel implant

Biochem/physiol Actions

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.

Warning

Toxicity: Harmful (C)

Unit Definition

One unit is determined by comparison with a standard curve prepared using the Bureau of Biologics standard thrombin.

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

Prepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 2 months at -70°C.

Analysis Note

Complete activation from homogeneous prothrombin by SDS-PAGE

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.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

605190-100U-M:
605190-100U:
605190-1000U:
605190-1000U-M:
605190-5TU-M:
605190-5TU:
605190-1000RU:
605190-100RU:
605190-U:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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