Proteinase K - Highly Purified Serine Protease for Molecular Biology Applications

REF #: 3200505
Short description
  • Highly purified serine protease (Proteinase K) for molecular biology applications
  • Ideal for proteolytic inactivation of nucleases during DNA and RNA isolation
  • Main activity: 30 units/mg protein
  • Derived from Tritirachium album (Endopeptidase K)
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  • Procurenet Team Tshim Sha Tsui
    Hong Kong Hong Kong 3 years
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  • 7 Days Return Back Policy
  • 2 Days Cancellation Policy
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Proteinase K - Highly Purified Serine Protease for Molecular Biology Applications

Proteinase K, also known as Endopeptidase K, is a highly purified serine protease derived from Tritirachium album. With a main activity of 30 units per milligram of protein, it is widely used for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. Its ability to specifically cleave peptide bonds in proteins makes it an essential tool in various molecular biology applications.

  • Purity: Proteinase K is highly purified to ensure maximum activity and minimal interference with other biochemical reactions. This high level of purity guarantees reliable and consistent results in various applications.
  • Specificity: As a serine protease, Proteinase K exhibits remarkable specificity in cleaving peptide bonds adjacent to aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. This specificity allows for efficient and precise digestion of proteins without non-specific cleavage.
  • Activity Range: Proteinase K is active in a broad range of conditions, including a wide pH range from 4.0 to 12.5 and temperatures from 20°C to 65°C. This versatility enables its application in various protocols and ensures optimal enzyme activity under different experimental conditions.
  • Stability: Proteinase K is highly stable, retaining its activity even in denaturing conditions, such as high temperatures or the presence of denaturing agents like SDS or urea. This stability allows for its use in applications that require harsh conditions or extended incubation times.
  • Solubility: Proteinase K is readily soluble in water and is compatible with a variety of buffers commonly used in molecular biology. Its solubility facilitates easy preparation of working solutions and allows for uniform distribution of the enzyme in reaction mixtures.
  • Applications: Proteinase K is commonly used in a wide range of molecular biology applications, including:
  • DNA and RNA isolation: Proteinase K is particularly useful for the inactivation of nucleases during DNA extraction and RNA isolation procedures. Its ability to efficiently degrade proteins, including those that may carry nucleases, helps ensure the integrity and purity of isolated nucleic acids.
  • Protein purification: Proteinase K can be used to remove unwanted protein contaminants or to digest target proteins for purification purposes. Its specificity allows for controlled digestion without non-specific degradation of the target protein.
  • Enzyme inactivation: Proteinase K can be used to inactivate various enzymes, including nucleases, proteases, and kinases. Its robust proteolytic activity can effectively neutralize enzymatic activity, providing a reliable method for enzyme deactivation.
  • Microbiological research: Proteinase K is often used in microbiological research for the digestion of cell walls and membranes. Its ability to efficiently break down these structures enables the release of intracellular components for further analysis.
  • Cellular and tissue imaging: Proteinase K can be employed in cell and tissue imaging techniques to enhance antigen retrieval, improve antibody penetration, or facilitate the removal of unwanted proteins or structures.

With its versatility, specificity, and stability, Proteinase K has become an indispensable tool in molecular biology research and a vital component in various laboratory protocols. Whether it's DNA and RNA isolation, protein purification, enzyme inactivation, or microbiological research, Proteinase K offers researchers a reliable and efficient solution for their molecular biology needs.

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