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> Recombinant Protein > Human Cell Expressed > SerpinF2 / SERPINF2 Protein (His Tag) SerpinF2 / SERPINF2 Protein (His Tag)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 10297-H08H |
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Alpha-2-antiplasmin ( SerpinF2 / SERPINF2 / AAP ) Protein
SerpinF2 / SERPINF2 / AAP Protein Price Inquiry ( Available Sizes )
- 50μg: Inquiring Price;
- 200μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
SerpinF2 / SERPINF2 / AAP Protein 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 |
| Source: | Human |
| Expression Host: | Human Cells |
SerpinF2 / SERPINF2 / AAP Protein QC Testing
| Purity: | > 97 % as determined by SDS-PAGE | SDS-PAGE:![]() Serpin F2 protein |
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Bio-activity: |
Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate,Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Anaspec, Catalog#27114) |
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| 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 | |
| Molecular 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 |
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| Formulation: | Lyophilized from sterile 25mM Tris, 150mM NaCl, pH 7.5
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SerpinF2 / SERPINF2 / AAP Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. 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 / SERPINF2 / AAP Protein Related Products & Topics
Related Areas:
Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Serpin Superfamily>>SerpinF2
Immunology>>Innate Immunity>>Coagulation>>SerpinF2
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| SerpinF2 | Human | SerpinF2 Protein, Recombinant![]() |
10297-H08H |
| SerpinF2 | Mouse | SerpinF2 Protein, Recombinant |
50167-M08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Human SerpinF2 |
WB, ELISA | SerpinF2 Antibody, Mouse MAb | 10297-MM05 |
| Human SerpinF2 |
WB, ELISA | SerpinF2 Antibody, Rabbit PAb | 10297-RP01 |
| Human SerpinF2 |
WB, ELISA | SerpinF2 Antibody, Rabbit PAb (Antigen Affinity Purified) | 10297-RP02 |
| Mouse SerpinF2 |
WB, ELISA | Rabbit Monoclonal Antibody | 50167-R128 |
| Mouse SerpinF2 |
WB, ELISA | Rabbit Polyclonal Antibody | 50167-RP01 |
| Mouse SerpinF2 |
WB, ELISA | Rabbit Polyclonal Antibody (Antigen Affinity Purified) | 50167-RP02 |
SerpinF2 / SERPINF2 / AAP Protein Description
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 at moderate level in other tissues such as muscle, intestine, central nervous system and placenta. 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. Alpha-2 AP plays the dominant role in inhibiting both plasma clot lysis and thrombus lysis, and accordingly, the deficiency of Alpha-2 antiplasmin in humans results in uncontrolled fibrinolysis and a bleeding disorder.
References
- Potempa, J. et al., 1988, Science. 241: 699-700.
- Menoud, P.A. et al., 1996, J. Clin. Invest. 97: 2478-2484.
- Mutch, NJ. et al., 2007, J. Thromb. Haemost. 5: 812-817.
- Victoria, J. et al., 2007, Blood, 109: 5286-5292.
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