Recombinant Human Serpin C1/Antithrombin-III Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit Recombinant Human Coagulation Factor II/Thrombin (Catalog # 1473-SE) cleavage of a fluorogenic peptide substrate Boc-VPR-AMC (Catalog # ES011). The IC50 value is <5 nM, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived human Serpin C1/Antithrombin-III protein His33-Lys464, with a C-terminal 10-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
50 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Serpin C1/Antithrombin-III Protein, CF
serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
serine-cysteine proteinase inhibitor clade C member 1
serpin peptidase inhibitor, clade C (antithrombin), member 1
Serpin C1 is a member of the Serpin superfamily of the serine protease inhibitors (1). It is the principal plasma Serpin of blood clotting proteases and inhibits thrombin as well as several factors such as Xa (2). Similar to Serpins A5 and D1, its thrombin inhibitory activity is enhanced by heparin. Hereditary and acquired Serpin C1 deficiency is the cause of an increased thrombotic tendency in many cases (3). For example, acquired Serpin C1 deficiency is a common condition in sepsis, after major trauma or surgery (4).
Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
Chuang, Y.-J. et al. (2001) Biochemistry 40:6670.
Vinazzer, H. (1999) Semin. Thromb. Hemost. 25:257.
Risberg, B. (1998) Blood Coagul. Fibrinolysis Suppl. 3:S3.
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