Elastase, lyophilized, 100 mg, glass

Porcine pancreatic elastase is a serine protease with a molecular mass of 25.9 kDa and an optimal catalytic pH of 8.5. The enzyme hydrolyzes peptide bonds on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, valine, leucine, and isoleucine, and additionally exhibits activity toward amides and esters, e.g., N-benzoyl-L-alanyl methyl ester.

A defining feature of elastase is its ability to cleave native elastin, a substrate not degraded by trypsin, chymotrypsin, or pepsin. It also hydrolyzes other proteins, including fibrin, casein, hemoglobin, albumin, and denatured collagen. Proteolytic activity can be inhibited by soybean trypsin inhibitor or kallikrein inhibitor, while elastolytic function remains unaffected. Due to this substrate specificity, elastase is frequently used in combination with other proteases for enzymatic cell dissociation, enabling efficient isolation of cells from animal tissues or culture surfaces.