Thermolabile Proteinase K is an engineered, subtilisin-related serine protease that will hydrolyze a variety of peptide bonds. It preferentially cleaves the peptide bond at the carboxyl side of aliphatic or aromatic amino acid residues. However; the specificity of Thermolabile Proteinase K can be broad.
Thermolabile Proteinase K is an engineered, subtilisin-related serine protease that will hydrolyze a variety of peptide bonds. It preferentially cleaves the peptide bond at the carboxyl side of aliphatic or aromatic amino acid residues. However; the specificity of Thermolabile Proteinase K can be broad.
Thermolabile Proteinase K (TLPK) can be completely inactivated by incubation at 55°C for 10 minutes, which allows for subsequent enzymatic steps in the same reaction vessel. Figure 1 shows that the activity of restriction endonucleases, including heat-stable endonucleases, can be completely abolished using TLPK.
Product Source
Cloned from Engyodontium album (formerly Tritirachium album), mutagenized to increase thermolability of the enzyme and expressed in Pichia pastoris.
Price | 990,00 RON (preturile sunt fara TVA) |
---|---|
Description |
Thermolabile Proteinase K is an engineered, subtilisin-related serine protease that will hydrolyze a variety of peptide bonds. It preferentially cleaves the peptide bond at the carboxyl side of aliphatic or aromatic amino acid residues. However; the specificity of Thermolabile Proteinase K can be broad.
Product Source Cloned from Engyodontium album (formerly Tritirachium album), mutagenized to increase thermolability of the enzyme and expressed in Pichia pastoris. |