Abcam, ab281339, Recombinant Proteinase K (Active)

Size: 100mg
Recombinant Proteinase K (Active) is a Parengyodontium album Full Length protein, in the 106 to 384 aa range, expressed in Yeast, with >95%, < 0.25 EU/mg endotoxin level, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>95% SDS-PAGE,
Endotoxin level:< 0.25 EU/mg,
Expression system:Yeast,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity >30 units/mg.,
Accession:P06873,
Animal free:Yes,
Carrier free:No,
Species:Parengyodontium album,
Reconstitution:Reconstitute in water,
Storage buffer:pH: 8Constituents: 6% Trehalose, 0.32% Tris HCl

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
Biological function summary
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.
Pathways
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.