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Thrombin from bovine plasma

powder, suitable for cell culture, ≥1,500 NIH units/mg protein (E1%/280 = 19.5)

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



specific activity

≥1,500 NIH units/mg protein (E1%/280 = 19.5)

mol wt

heavy chain ~31 kDa
light chain ~6 kDa


cell culture | mammalian: suitable

UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

cow ... F2(280685)

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General description

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.


Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess an expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.

Biochem/physiol Actions

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, and is measured by direct comparison to an NIH thrombin reference standard.


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.

Analysis Note

The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL 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.
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard, Lot K.

Other Notes

View more information on thrombin at


Exclamation markHealth hazard

Signal Word


Hazard 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



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

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More Documents

Quotes and Ordering

Zachary T Britton et al.
Protein expression and purification, 84(2), 224-235 (2012-06-23)
Biophysical and structural characterization of G protein-coupled receptors (GPCRs) has been limited due to difficulties in expression, purification, and vitro stability of the full-length receptors. "Divide and conquer" approaches aimed at the NMR characterization of peptides corresponding to specific regions
Yuya Nakatani et al.
Archives of oral biology, 73, 172-178 (2016-10-25)
Platelet-rich plasma (PRP) is typically isolated and applied immediately after preparation, making it both a time- and labor-intensive addition to the operative procedure. Thus, it would be convenient if PRP could be preserved. We evaluated the efficacy of freeze-dried PRP
Sharon Wei Ling Lee et al.
Advanced healthcare materials, 9(7), e1901486-e1901486 (2020-03-04)
Polymer nanoparticles (NPs), due to their small size and surface functionalization potential have demonstrated effective drug transport across the blood-brain-barrier (BBB). Currently, the lack of in vitro BBB models that closely recapitulate complex human brain microenvironments contributes to high failure
Mikaël M Martino et al.
Biomaterials, 30(6), 1089-1097 (2008-11-26)
The extracellular matrix (ECM) exerts powerful control over many cellular phenomena, including stem cell differentiation. As such, design and modulation of ECM analogs to ligate specific integrin is a promising approach to control cellular processes in vitro and in vivo
Herbert Nar
Trends in pharmacological sciences, 33(5), 279-288 (2012-04-17)
The quest for novel medications to treat thromboembolic disorders such as venous thrombosis, pulmonary embolism and stroke received a boost when the 3D structures of two major players in the blood coagulation cascade were determined in 1989 and 1993. Structure-guided

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