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Highly active and stable endopeptidase purified from the fungus T. album
Proteinase K is a highly active and stable endopeptidase used in a wide range of applications purified from the fungus T. album. It cleaves peptide bonds mainly following the carboxyl group of N-substituted hydrophobic aliphatic and aromatic amino acids(1) and is classified as a serine protease. Proteinase K is useful in purifying high molecular weight nucleic acids from cells and tissues (i.e. genomic DNA isolation from mouse tails) and in revealing protein structure and function.
Molecular Weight: 28.9 kDa
Optimum pH: 4.0-12.5(1)
Optimum Temperature: 65°C(1)
Working Concentration: 0.05 - 1 mg/ml
Activators: Stimulated by 0.2 - 1% SDS or 1 - 4M urea(8)
Inactivated by PMSF(1); Not inactivated by EGTA, thiol reagents or trypsin/chymotrypsin inhibitors(1)
Tested for contaminating ribonucleases and deoxyribonucleases.
One unit is the amount of enzyme that liberates folin positive amino acids and peptides corresponding to 1 μmol tyrosine in 1 min at 37°C using hemoglobin as substrate.
20 - 50 units/mg
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- CROWE, J. S., COOPER, H., SMITH, M., SIMS, M., PARKER, D. AND GEWERT, D. (1991) Nucl. Acids. Res. 19, 184.
- Used in the isolation of native, high molecular weight DNA and RNA.
- Used as a general protease to inactivate DNases, RNases and to degrade proteins.
- Specifically modifies cell surface proteins and glycoproteins for analysis of membrane structures for protein localization(5,6).
- Produces characteristic protein fragments used in enzyme/protein structure and function studies(7).
Shipped on cold pack. Store dry at 4°C.
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