Mouse SerpinF2 Protein (His Tag)

Mouse Serine (or cysteine) Peptidase Inhibitor Clade F Member 2 Protein

SerpinF2 Protein Product Information

• Synonym: Serpinf2 ,RP23-384C18.2, AI747498, Pli, Serpimf2
• Protein Construction: A DNA sequence encoding the mouse Serpin F2 ( NP_032904.1 ) ( Met 1 - Lys 491 ) was expressed with a C-terminal polyhistidine tag
• Source: Mouse
• Expression Host: Human Cells

SerpinF2 Protein QC Testing

• Purity: > 97% as determined by SDS-PAGE
• Bio-activity: Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 ( Anaspec, Catalog#27114 )
  The IC₅₀ value is < 0.5 nM as measured in 100μL reaction mixture containing 1.25 ng trypsin ( Sigma, Catalog#T1426 ), 10 μM substrate, 50 mM Tris , 10 mM CaCl₂ , 0.15 M NaCl , pH 7.5
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Val 28
• Molecular Mass: The secreted recombinant mouse Serpin F2 consists of 475 amino acids and has a calculated molecular mass of 53.6 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 60-65 kDa protein in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: SerpinF2 protein

SerpinF2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃ immediately after receipt. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

SerpinF2 Protein Description

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Over 1000 serpins have been identified including 36 human proteins. As a member of the Serpin superfamily and the primary physiological inhibitor of the serine protease plasmin, Serpin F2 is responsible for the dissolution of fibrin clots. Serpin F2 is mainly expressed by liver and kidney, while other tissues such as muscle, intestine, central nervous system, and placenta also express this protein at a moderate level. It is indicated that Serpin F2 is a key regulator of plasmin-mediated proteolysis in these tissues. Mouse Serpin F2 is synthesized as a 491 amino acid precursor with a 27 amino acid signal peptide, a short propeptide (28 to 39) and a mature chain (40 to 491).

References

1. Sumi, Y. et al., 1989, J. Biochem. 106: 703-707.
2. Menoud, P. A. et al., 1996, J. Clin. Invest. 97: 2478-2484.
3. Silverman, G.A. et al., 2001, J. Biol. Chem. 276: 33293-33196.
4. Irving, J. et al., 2002, Mol Biol Evol. 19 (11): 1881-1890.
5. Rawlings, N.D. et al., 2004, Biochem J. 378: 705-716.
6. Filleur, S. et al., 2009, J Cell Biochem. 106 (5): 769-775.