Proteinase K is a nonspecific serine protease that hydrolyzes a variety of peptide bonds. This recombinant form of proteinase K is similar to the wild type, but with increased specificity and stability at room temperature (RT). Proteinase K is active on a wide range of temperatures and buffers with optimal activity between 15 and 75°C and pH between 4 and 11. Activity is stimulated with SDS, urea and EDTA buffers.
- Lyophilized White Powder.
- Isolated from a recombinant yeast expressing modified gene of Tritirachium limber.
- 20 mM Tris-HCl, 1 mM CaCl , 50% glycerol or dH O, pH7,4 at 25°C. Molecular Weight: 29,3 kDa.
- Store at -20ºC.
ACTIVITY ASSAY AND UNIT DEFINITIONS
One unit will release 1 μmol of tyrosine per minute at 37º C, pH7.5. Dnase and Rna Activity: not detectable. Special quality to use in molecular biology applications as well as all electrophoresis techniques.
- Isolation of DNA and RNA in a broad variety of tissues
- Glycoprotein modification in structural studies
- PCR purification; Inactivation of RNAses
- DNAses and enzymes in reaction.
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