Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl-containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants, and by Co2+, Cu2+, Cd2+, and heavy metal ions. Recombinant Lysobacter Enzymogenes Arg-C is a 26.8 kDa protease consisting of 252 amino acid residues including a C-terminal His-Tag.
Amino Acid Sequence
Hi-5 Insect cells
The reaction is measured as an increase in absorbance at 253 nm resulting from the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE).
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
For best results use only freshly reconstituted protease. Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Arg-C is activated by DTT, Cysteine, or other sulfhydryl containing reagents. The presence of calcium ions is essential. Arg-C is inhibited by oxidizing agents and sulfhydryl reactants and by Co2+, Cu2+, Cd2+, and heavy metal ions.