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Human SerpinF2 / SERPINF2 Protein (His Tag)

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SerpinF2Protein Product Information
Synonym:SerpinF2, AAP, API, PLI, α-2 AP, ALPHA-2-PI
Protein Construction:A DNA sequence encoding the human SerpinF2 (NP_000925.2) (Met 1-Lys 491) was expressed, with a C-terminal polyhistidine tag.
Expressed Host:Human Cells
Form & Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
SerpinF2Protein 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 .
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:Met 28
Molecule Mass:The recombinant human SerpinF2 consists of 475 amino acids after removal of the signal peptide and predicts a molecular mass of 53.2 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rhSerpinF2 is approximately 70 kDa due to glycosylation.
Formulation:Lyophilized from sterile 25mM Tris, 150mM NaCl, pH 7.5
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.
SerpinF2Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. 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, also known as alpha-2 antiplasmin (alpha-2 AP), is a member of the Serpin superfamily. SerpinF2 is the principal physiological inhibitor of serine protease plasmin, and as well as, an efficient inhibitor of trypsin and chymotrypsin. This protease is produced mainly by liver and kidney, and also expressed in 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. Alpha-2 AP is an unusual serpin in that it contains extensive N- and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. SerpinF2 is one of the inhibitors of fibrinolysis, which acts as the primary inhibitor of plasmin(ogen). It is a specific plasmin inhibitor, and is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. Alpha-2 AP plays the dominant role in inhibiting both plasma clot lysis and thrombus lysis, and accordingly, the congenital deficiency of Alpha-2 antiplasmin causes a rare bleeding disorder because of increased fibrinolysis. Thus, it may be a useful target for developing more effective treatment of thrombotic diseases.

  • Lee KN, et al. (2004) Alpha2-antiplasmin: potential therapeutic roles in fibrin survival and removal. Curr Med Chem Cardiovasc Hematol Agents. 2(4): 303-10.
  • Matsuno H. (2006) Alpha2-antiplasmin on cardiovascular diseases. Curr Pharm Des. 12(7): 841-7.
  • Burnouf T, et al. (2007) Impact of Triton X-100 on alpha 2-antiplasmin (SERPINF2) activity in solvent/detergent-treated plasma. Biologicals. 35(4): 349-53.
  • Carpenter SL, et al. (2008) Alpha2-antiplasmin and its deficiency: fibrinolysis out of balance. Haemophilia. 14(6): 1250-4.
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