ELASTASE FROM PORCINE PANCREAS, LYOPHIL&

Description_x000D_ General description_x000D_ Elastase is a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges. The molecular mass is approximately 25.9kDa. The enzyme is synthesized as an inactive zymogen, proelastase, which is converted to the active form by limited proteolysis at the N-terminal by trypsin._x000D_ Application_x000D_ Elastase from porcine pancreas is used for the following applications:_x000D_ • Cell culture techniques_x000D_ • ELISA techniques_x000D_ • Used in assay for elastase inhibitory activity_x000D_ Packaging_x000D_ 1, 5 mg in glass bottle_x000D_ Package size based on protein content_x000D_ 20 mg in poly bottle_x000D_ Biochem/physiol Actions_x000D_ Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin._x000D_ Enzyme that degrades elastin, a matrix component of tissues involved in stretching processes. It is a serine protease with broad specificity. It cleaves protein at the carboxyl side of small hydrophobic amino acids such as Ile, Gly, Ala, Ser, Val, and Leu. The enzyme also hydrolyzes amides and esters such as N-Benzoyl-L-alanine methyl ester._x000D_ Unit Definition_x000D_ One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.