Thrombin from human plasma

lyophilized powder, ≥1,000 NIH units/mg protein (E1%/280, 18.3)

Factor IIa
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:


lyophilized powder

Quality Level

specific activity

≥1,000 NIH units/mg protein (E1%/280, 18.3)

mol wt

37.4 kDa


HIV and HBsAg, source material tested negative

Featured Industry

Diagnostic Assay Manufacturing

UniProt accession no.

storage temp.


Gene Information

human ... F2(2147)

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General description

The F2 gene encodes thrombin protein and is mapped to human chromosome 11p11.2.


Thrombin from human plasma has been:
  • dissolved in CaCl2 and added to poly ethylene glycolated fibrinogen/cell solution for fibrin production
  • to polymerize fibrin on well plates
  • used as an endogenous agonist proteinase for proteinase-activated receptors : PAR1, PAR3 and PAR4 for stimulation of cells

Biochem/physiol Actions

Thrombin is an endolytic serine protease which stimulates vascular damage induced-leukocytes, platelets, endothelial and mesenchymal cell production. This action is mediated via G-protein-coupled receptor. It catalysis the cleavage of fibrinogen at Arg−Gly bonds to form fibrin and release fibrinopeptides A and B. The predominant form of thrombin in vivo is the zymogen prothrombin (factor II), which is produced in the liver. Prothrombin is a coagulation activation factor, high levels of which indicates cancer. Thrombin can be used to cleave fusion proteins. Cleavage of fusion proteins can be carried out at a thrombin:fusion protein ratio of 1:500.
Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.

Unit Definition

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard

Physical form

Lyophilized from saline sodium citrate buffer, pH 6.5

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.

Other Notes


Health hazard





NONH for all modes of transport

WGK Germany


Flash Point F

Not applicable

Flash Point C

Not applicable

Certificate of Analysis

Certificate of Origin

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. What is the cross reactivity of Thrombin?

    Thrombin from any vertebrate species will clot the fibrinogen of virtually any other species.  Fibrinogen from any mammalian source will cross-react with thrombin from any mammalian source, but it is not well known how thrombin and fibrinogen from different animals differ in their sequence.  When any mammalian thrombin is injected into a different mammal, clotting will occur.

  6. For thrombin, how do NIH units compare to International Units (IU)?

    One NIH unit of thrombin is equivalent to approximately 1.8 International Unit (IU) of thrombin.

  7. What is the solubility of Product T7009, Thrombin from human plasma?

    Thrombin from human plasma gave a clear very faint yellow solution when dissolved at 100 unit vial plus 1 ml of 28 mM sodium barbital, 0.125M sodium chloride, 1% BSA, 0.5% PEG, pH 7.35.  Thrombin from bovine plasma (T4648) is soluble in water at 10 mg/mL.

  8. What is the solution stability of Product T7009, Thrombin from human plasma?

    By analogy to thrombin from bovine plasma (T4648), we expect stock solutions of thrombin from human plasma to be stable for one week kept refrigerated at 2-8° C. Since thrombin solutions adsorb to glass, it is recommended to aliquot the solutions in plastic tubes and store frozen at -20°C or colder for long term storage.

  9. What is the isoelectric point of Product T7009, Thrombin from human plasma?

    The isoelectric point (pI) range of the human thrombin isozymes is 6.35 - 7.6. The major isoform has a pI of 7.31.

  10. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

Signal transduction for proteinase-activated receptor-2-triggered prostaglandin E2 formation in human lung epithelial cells
Kawao N, et al.
Journal of Pharmacology and Experimental Therapeutics, 315(2), 576-589 (2005)
New vectors for high level expression of recombinant proteins in bacteria
Hakes DJ and Dixon JE
Analytical biochemistry, 202(2), 293-298 (1992)
Protease-activated receptor 3 is a second thrombin receptor in humans
Ishihara H, et al.
Nature, 386(6624), 502-502 (1997)
Capillary-like network formation by human amniotic fluid-derived stem cells within fibrin/poly (ethylene glycol) hydrogels
Benavides OM, et al.
Tissue Engineering: Part A, 21(7-8), 1185-1194 (2015)
Epidemiology and pathophysiology of cancer-associated thrombosis
Noble S and Pasi J
British Journal of Cancer, 102(S1), S2-S2 (2010)
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