rhSerpin F2

Lyophilized. Lyophilized from sterile-filtered 150 mM NaCl, 25 mM Tris-HCl, pH 7.5. Full-length, recombinant, human serpin F2 (amino acids 1-491) fused at the C-terminus to a 10X His•Tag^® sequence and expressed in NS0 cells. The presence of the pro-domain does not affect plasmin inhibition, but reduces cross-linking to fibrin. A member of the Serpin superfamily of the serine protease inhibitors that is responsible for the dissolution of fibrin clots. It is also an efficient inhibitor of trypsin and chymotrypsin. Liver and kidney are the predominant sites for expression, but other tissues such as muscle, intestine, CNS, and placenta also express serpin F2 mRNA at moderate levels. The tissue distribution implicates serpin F2 as a key regulator of plasmin-mediated proteolysis in these tissues. Biological activity: Inhibition of plasmin cleavage: IC₅₀ <13 nM as meaured by the inhibition of cleavage of 10 µM MCA-Arg-Pro-Lys-Pro-Val-Glu-Nval-Trp-Arg-Lys(Dnp)-NH₂ by 6.4 nM plasmin in 150 mM NaCl, 50 mM Tris-HCl, 10 mM CaCl₂, pH 7.5. Inhibition of trypsin cleavage: IC₅₀ <10 nM as measured by inhibition of cleavage of the above substrate by 2.3 nM trypsin in 150 mM NaCl, 50 mM Tris-HCl, 10 mM CaCl₂, pH 7.5.. Purity: ≥95% by SDS-PAGE. Contaminants: Endotoxin: ≤1 EU/µg protein.

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