Proteinase K enzyme

Proteinase K is a tetilisin-dependent serine endopeptidase that hydrolyzes a variety of peptide bonds. Proteinase K is active in different conditions of temperature and buffer with optimal activity between 20 and 60 °C and pH between 7.5 and 12.0.

Applications of proteinase K:

Isolation of plasmid and genomic DNA

Isolation of RNA

Deactivation of RNases, DNases and enzymes in reactions

Removal of enzymes from DNA to improve cloning efficiency

PCR purification

Isolation of mitochondria

Eliminating endotoxins dependent on cationic proteins, such as lysozyme and ribonuclease A

Determination of enzyme localization on membranes

Exposure of antigen binding sites in paraffin-embedded tissue sections for antibody labeling

Digestion of proteins from brain tissue samples

Promotion of cell lysis by activation of a bacterial autolytic factor

Analysis of membrane structure by modifying proteins and glycoproteins on cell surfaces

Isolation of nucleic acids for amplification reactions

To remove cellular debris during the preparation of colony lifts, and to treat tissue sections to ensure efficient probe penetration.