Recombinant Proteinase K is a Parengyodontium album Full Length protein, with >=99% purity and suitable for FuncS.
Application | Reactivity | Dilution info | Notes |
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Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Hydrolyzes keratin at aromatic and hydrophobic residues.
Proteinase K, Endopeptidase K, Tritirachium alkaline proteinase, PROK
Recombinant Proteinase K is a Parengyodontium album Full Length protein, with >=99% purity and suitable for FuncS.
pH: 7.4
Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
Hydrolyzes keratin at aromatic and hydrophobic residues.
Belongs to the peptidase S8 family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This product is manufactured by BioVision, an Abcam company and was previously called 9211 Proteinase K, Recombinant, 20 mg/ml Solution, Molecular Grade. 9211-5 is the same size as the 5 ML size of ab286007. 9211-25 is the same size as the 25 ML size of ab286007. 9211-100 is the same size as the 100 ML size of ab286007.
Proteinase K also known by alternate names like pronase dako proteinase K prokeinase K protein K and protease K is a serine protease widely used in molecular biology. This enzyme derived from the fungus Engyodontium album has a molecular mass of approximately 28.9 kDa. Proteinase K demonstrates high proteolytic activity effectively breaking down proteins by cleaving peptide bonds adjacent to the carboxyl group of aliphatic and aromatic amino acids. Researchers often utilize this enzyme in DNA and RNA purification protocols due to its ability to inactivate nucleases. It is typically expressed in microbial or cell-free systems optimized for high yield and activity.
Proteinase K plays a critical role in protein degradation. It exhibits robust activity even in the presence of detergents and high temperatures characteristics that make it a powerful tool in the removal of proteins during nucleic acid isolation. This enzyme is not a part of any complex within the organism but acts independently in protein digestion processes. Its ability to function under extreme conditions expands its utility across various biological applications.
Proteinase K engages in pathways related to protein catabolism and turnover. It does not contribute directly to metabolic pathways within living organisms; however it assists experimental pathways in vitro by efficiently degrading proteins. Proteinase K's proteolytic capabilities make it instrumental in preventing protein contamination aiding the study of valid biological interactions without extraneous protein interference. Related proteins like pepsin and trypsin also participate in protein degradation but they have different activity profiles and optimal conditions.
Proteinase K is frequently employed in research on genetic disorders and infectious diseases. While the enzyme itself is not associated with causing diseases its role in DNA and RNA extraction is vital for diagnosing conditions such as hereditary diseases and viral infections. Through these processes Proteinase K indirectly interacts with proteins relevant to diseases like cystic fibrosis and HIV. By facilitating the isolation of pure nucleic acids Proteinase K supports studies aiming to elucidate the genetic and viral proteins connected with these disorders.
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