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 # <a class=NoLineLink href='http://www.rndsystems.com/product_results.aspx?k=1473-SE'>1473-SE</a>) cleavage of a fluorogenic peptide substrate Boc-VPR-AMC (Catalog # <a class=NoLineLink href='http://www.rndsystems.com/product_results.aspx?k=ES011'>ES011</a>).<br />The IC<SUB>50</SUB> value is <5 nM, as measured under the described conditions. <br /><br />
<1.000 EU per 1 µg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Inhibition Activity
Theoretical MW
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.
SDS-PAGE
55-65 kDa, reducing conditions
Publications
Read Publications using 1267-PI in the following applications:
Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 25 mM MES, 150 mM NaCl, pH 6.5.
Notes
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
Antithrombin-III
AT3antithrombin-III
ATIII
ATIIIantithrombin III
MGC22579
serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
serine-cysteine proteinase inhibitor clade C member 1
Serpin C1
serpin peptidase inhibitor, clade C (antithrombin), member 1
Background
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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