Elastase is a serine protease consisting of a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges (Shotton & Hartley). Elastase is synthesized as a zymogen (proelastase) and is converted to the active form by limited trypsin proteolysis at its N-terminal. Elastase preferentially cleaves the peptide bond of C-terminal neutral, non-aromatic amino acid residues (Schellenberger et al.). Elastase is frequently used in combination with other proteases such as collagenase and trypsin to digest fibrous tissues because of its ability to digest native elastin.
Elastoproteinase; Lysosomal elastase; Pancreatic elastase I; Pancreatopeptidase E
Epithelial Cells; Myogenic Stem and Progenitor Cells
Human; Mouse; Rat; Non-Human Primate; Other
Area of Interest:
Cancer Research; Endothelial Cell Biology; Epithelial Cell Biology; Immunology; Stem Cell Biology
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