Trypsin, Modified, Sequencing Grade
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Specification
Product Description
Lyophilized. Purified. TPCK treated. Autolysis products free.
Biological function
Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from inactive precursor zymogen, trypsinogen.
Host
Bovine
Form
Lyophilized
Preparation Method
Native protein purified from Bovine Pancreas. Further chemically modified to promote stability and purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.
Activity
>=4 units per mg protein. One Unit is equivalent to one micromole of TCA soluble products, measured as tyrosine, released from 2% casein per minute, in 0.05 M Tris-HCl, pH 7.6, at 37°C, in a 30 minute reaction.
Recommend Usage
Tissue dissociation (combined with other enzymes); Cell harvesting by trypsinization; Mitochondria isolation; in vitro studies of proteins; Various hemagglutination procedures; Sample preparation for flow cytometric DNA analysis; Tryptic mapping; Fingerprinting and sequencing work; Environmental monitoring; Subculturing cells; Cleavage fusion proteins; Generating glycopeptides from purified glycoproteins.
Storage Instruction
Store at -20°C on dry atmosphere.
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Applications
Enzyme Activity
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Gene Info — PRSS2
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Gene Info — PRSS1
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Publication Reference
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Optimal computational comparison of mass spectrometric peptide profiles of alternative hydrolysates from the same starting material.
Holton TA, Dillon ET, Robinson A, Wynne K, Denis C. Shields DC.
LWT-Food Science and Technology 2016 Nov; 73:296.
Application:Enzyme, Recombinant protein.
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Optimal computational comparison of mass spectrometric peptide profiles of alternative hydrolysates from the same starting material.
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