Recombinant Mouse Alpha 2 Antiplasmin / A2AP Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0158
Recombinant Mouse Alpha 2 Antiplasmin / A2AP Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0158
Catalog No.: BLPSN-0158
Product Overview
| Tag | His |
| Host Species | Mouse |
| Accession | NP_032904.1 |
| Synonym | AI747498, Pli, Serpimf2 |
| Background | 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. |
| Description | A DNA sequence encoding the mouse Serpin F2 (NP_032904.1) (Met 1-Lys 491) was expressed with a C-terminal His tag. |
| Source | HEK293 |
| Predicted N Terminal | Val 28 |
| AA Sequence | Met 1-Lys 491 |
| Molecular Weight | The secreted recombinant mouse Serpin F2 consists of 475 a.a. 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. |
| Purity | >97% as determined by SDS-PAGE |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
| Bioactivity | 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 100uL reaction mixture containing 1.25 ng trypsin (Sigma, Catalog#T1426), 10 uM substrate, 50 mM Tris, 10 mM CaCl2, 0.15 M NaCl, pH 7.5. |
| Formulation | Lyophilized from sterile PBS, pH 7.4. |
| Stability | The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. |
| Usage | For Research Use Only |
| Storage | Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
