Mouse myeloma cell line, NS0-derived mouse Plasma Kallikrein/KLKB1 protein Gly20-Ala638, with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Predicted Molecular Mass
80 kDa, reducing conditions
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002). The specific activity is >300 pmol/min/µg, as measured under the described conditions.
Formulation, Preparation and Storage
Supplied as a 0.2 μm filtered solution in MES and NaCl.
The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after opening.
Background: Plasma Kallikrein/KLKB1
Plasma kallikrein, a serine protease, is synthesized in the liver and circulates in the plasma by binding to high molecular weight (HMW) kininogen or as a free zymogen. Once activated by its physiological activator, factor XII, it displays endopeptidase activity towards peptide bonds after arginine (preferred) and lysine. It cleaves HMW kininogen, its major physiological substrate, to release the potent vasodilator peptide bradykinin. It is also able to cleave a number of inactive precursor proteins to generate active products, such as plasminogen and prourokinase. Thus, it plays an important role in blood pressure regulation, fibrinolysis, and neutrophil activation (1). Mouse plasma kallikrein precursor contains a signal peptide (residues 1 to 19) and a pro form sequence (residues 20 to 638). Upon activation, the pro form is converted to a heavy chain and a light chain, which is linked by disulfide bonds and the latter contains the catalytic domain (2). The mouse plasma kallikrein pro form was expressed in the NS0 cells with a foreign signal peptide. After being treated by thermolysin, the purified enzyme is active against a fluorogenic peptide substrate described in the Activity Assay Protocol.
Colman, R. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds. p. 1644.
Seidah, N. et al. (1990) DNA and Cell Biology 9:737.
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