Digest native elastin in cell cultures with Elastase. This serine protease is frequently used in combination with other proteases such as collagenase and trypsin to digest fibrous tissue. Elastase consists of a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges (Shotton & Hartley). It is synthesized as a zymogen (proelastase) and then 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.).
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Protocols and Documentation
Find supporting information and directions for use in the Product Information Sheet or explore additional protocols below.
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