金山科研平台，产品价格货期咨询微信：jinshanbio Source:Mouse myeloma cell line, NS0-derived, Glu25-Lys413, with a C-terminal 6-His tag Accession #:AAH11040 N-terminal Sequence Analysis:Glu25 Purity:>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 µg per lane. Endotoxin Level: Predicted Molecular Mass:44 kDa SDS-PAGE:50-60 kDa, reducing conditions Activity:Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH₂ (Catalog# ES002).The IC₅₀ is <5 nM, as measured under the described conditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris and NaCl.See Certificate of Analysis for details. Molecule Information: Serpin A1a Aliases: Aat2; Dom1; PI1; Spi1-1 Entrez Gene IDs: 5265 (Human); 20700 (Mouse) Background: Serpins The human serpin superfamily consists of at least 35 members that target not only serine proteases, but also selected cysteine proteases and non-protease proteins. Serpins bind the protease active site resulting in a major conformational rearrangement that traps the enzyme in a covalent acyl-enzyme intermediate. As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. They are also involved in activities that extend beyond their ability to inhibit proteases. For instance, they may also regulate blood pressure, angiogenesis, or act as storage/transport proteins.