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Recombinant Human Coagulation Factor II/Thrombin Protein, CF

Bio-Techne includes R&D Systems | Catalog # 1473-SE

Catalog #
Size / Price

Key Product Details



Accession #

Structure / Form

Active form




Enzyme Activity

Product Specifications


Mouse myeloma cell line, NS0-derived human Coagulation Factor II/Thrombin protein
Met1-Glu622 with a C-terminal 10-His tag
The proenzyme was purified, activated and further purified.


>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Thr328, Ile364 & Val515

Predicted Molecular Mass

4 kDa (light chain A), 31 kDa (heavy chain B), 14 kDa (C-terminal fragment)


12 kDa, 21 kDa and 23 kDa, reducing conditions


Measured by its ability to cleave the fluorogenic peptide substrate Boc-VPR-AMC (Catalog # ES011).
The specific activity is >20,000 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation and Storage

Formulation Lyophilized from a 0.2 μm filtered solution in HEPES and NaCl.
Reconstitution Reconstitute at 100 μg/mL in sterile 50 mM HEPES and 580 mM NaCl, pH 7.5.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Coagulation Factor II/Thrombin

Coagulation Factor II, commonly known as thrombin, is an essential component of the coagulation cascade in which it converts fibrinogen to fibrin, activates factors V, VII, VIII, XIII and forms complexes with protein C and thrombomodulin (1). It also activates platelets and regulates the behavior of additional cells through protease‑activated receptors (PARs) (2). It may have either protective or deleterious functions, depending on the level and location (3). Its activity is regulated by endogenous inhibitors such as anti-thrombin III (serpin C1) or heparin cofactor II (serpin D1). A plasma serine protease, thrombin is synthesized in the liver as a 622 amino acid precursor with a 24 amino acid signal peptide. Cleavage by itself or by similar enzymes converts the proenzyme to three forms designated as alpha‑,  beta‑ and  gamma‑thrombin. Composed of a disulfide bond-linked dimer of the light chain (A) (residues 328-363) and the heavy chain (B) (residues 364‑622), alpha-thrombin displays the diverse functions as described above. In comparison, the further processed B chains of beta- and gamma-thrombin have no known physiological function, but retain most of the activity towards small synthetic substrates (4). The recombinant human thrombin may be used to process proteins containing the thrombin cleavage site. The conditions for processing different proteins, such as the ratio of protein/thrombin, buffer components, temperature and time of incubation, may vary and should be empirically determined.


  1. Degen, S.J. and E.W. Davie (1987) Biochemistry 26:6165.
  2. Coughlin, S.R. (2000) Nature 407:258.
  3. Xi, G. et al. (2003) J. Neurochem. 84:3.
  4. Rydel, T.J. et al. (1994) J. Biol. Chem. 269:22000.

Alternate Names

F2, Thrombin

Entrez Gene IDs

2147 (Human); 14061 (Mouse)

Gene Symbol



Additional Coagulation Factor II/Thrombin Products

Product Documents for Recombinant Human Coagulation Factor II/Thrombin Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Coagulation Factor II/Thrombin Protein, CF

For research use only