Description General description Native elastase from porcine pancreas. A serine protase that catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin and of a number of synthetic substrates containing aspartic acid, phenylalanine, or tyrosine. Inhibited by DFP, elastinal, and α2-macroglobulin. Native elastase from porcine pancreas. Catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin, and of a number of synthetic substrates containing aspartic acid, glutamic acid, phenylalanine, or tyrosine. Preferentially cleaves peptide bonds at the carbonyl end of amino acid residues with small hydrophobic side chains, such as glycine, valine, leucine, isoleucine, and particularly alanine. Inhibited by DFP, elastinal, and α2-macroglobulin. Has an optimal pH of 7.8-8.5; pI = 9.5. Note: Elastase tends to adhere to glass. Hence, use of siliconized glassware is recommended. Packaging 1000, 250 u in Plastic ampoule Warning Toxicity: Standard Handling (A) Unit Definition One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Suc-Ala-Ala-Pro-Abu-pNA (Cat. No. 324699) per min at 25°C, pH 8.0. Physical form Lyophilized from 50 mM Trehalose, 1 mM Acetic Acid. Reconstitution Following reconstitution, elastase may be stored at 4°C at pH 6.0 for long term use. If incubated at room temperature at or near its optimum pH, elastase rapidly autolyzes to a mixture of peptides. Stock solutions are stable for up to 2 months at 4°C, pH 6.0. Other Notes Largman, C. et al. 1976. Biochemestry15, 2491. Mandl, I. 1962. Methods in Enzymol.5, 665.; Description