Description
Proteinase K from Tritirachium album. Chromatographically purified, free of ribo- and deoxyribonucleases.
Proteinase K is a non-specific serine protease with strong proteolytic activity on denatured (in SDS) and high molecular weight native proteins. It cleaves peptide bonds typically after the carboxyl group of N-substituted hydrophobic, aliphatic and aromatic amino acids.
- 25 µg proteinase K immobilized on matrix G3m per CR-column
- 0.7 mAnson units immobilized per CR-column
- CR-column cuts at least 370 µg BSA per application
- Columns are more active in 0.1% SDS and at 40°C, as well as PBS buffer
- Proteinase K with 200 µl matrix G3m, 1 column
- Storage buffer, 50 mM Tris/HCl, pH 7.5
- Reaction buffer, 50 mM Tris/HCl, 5 mM NaCl, pH 8.0
- Washing buffer, 50 mM Tris/HCl, 1.0 M NaCl, pH 8.0