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Cat. No.
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CPE07
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Description
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Elastase, like trypsin and chymotrypsin, is a serine protease that also hydrolyses amides and esters. It is produced in the pancreas as an inactive zymogen, proelastase, and activated in the duodenum by trypsin. Elastase is distinctive in that it acts upon elastin. Because elastin in found in highest concentrations in the elastic fibers of connective tissues, elastase is frequently used to dissociate tissues which contain extensive intercellular fiber networks.
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CAS No.
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9004-06-2
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Synonym
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pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; pancreatic elastase
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Reaction
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Hydrolysis of proteins, including elastin. Preferential cleavage: Ala
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Molecular Weight
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25,900Da
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Unit Definition
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One Unit cleaves one micromole of N-succinyl-L-alanyl-L-alanyl-L-alanine-p-nitroanilide per minute at 25°C, pH 8.0.
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Optimum pH
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8.5
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Isoelectric point
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8.5.
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Inhibitors
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DFP, elastinal, -2-macroglobulin.
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Stability
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Elastase is unstable below pH 3-4. When stored as a dry powder the enzyme is stable 6-12 months.
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Stability/Storage
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Elastase is unstable ≤ pH 3.5. When stored as a dry powder the enzyme is stable for 6-12 months at 2-8°C.
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Product Specification
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Appearance
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White or pale yellow lyophilized powder
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Activity
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≥ 30U/mg
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Loss on drying(60°C, 4 hours)
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≤ 6.0%
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Heavy metals(USP,E.P.)
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≤ 20 ppm
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Residue on ignition(USP,E.P.)
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≤ 1.0%
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Arsenic(USP,E.P.)
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≤ 2 ppm
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Conclusion: Product complies with the requirements from SFDA.
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