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Proteinase K Reagents Enzymes,
CAS 39450-01-6 Proteinase K
Proteinase K is an enzyme that belongs to the serine protease family. It is derived from the fungus Tritirachium album and has a broad range of applications in molecular biology and biochemistry. Proteinase K is known for its ability to degrade proteins by cleaving peptide bonds.
Here are some key features and applications of Proteinase K:
Broad specificity: Proteinase K exhibits a broad substrate specificity, meaning it can efficiently degrade a wide range of proteins, including native and denatured proteins.
Resistance to denaturing agents: Proteinase K remains active in the presence of denaturing agents such as urea, SDS (sodium dodecyl sulfate), and EDTA (ethylenediaminetetraacetic acid). This makes it particularly useful for protein extraction and purification protocols that involve denaturation steps.
DNA and RNA purification: Proteinase K is commonly used in DNA and RNA extraction protocols to remove proteins that are bound to nucleic acids. It helps in releasing DNA and RNA from their associated proteins, facilitating subsequent purification steps.
Tissue and cell lysis: Proteinase K is often employed in protocols for tissue and cell lysis, where it helps to break down the structural proteins and release the cellular components of interest. It is particularly effective in breaking down tough tissues, such as those found in seeds or environmental samples.
Inactivation of nucleases: Proteinase K can inactivate nucleases, enzymes that degrade nucleic acids. Therefore, it is commonly used in nucleic acid isolation procedures to ensure the integrity of DNA or RNA samples by degrading any contaminating nucleases.
Sterilization: Proteinase K can be utilized for the sterilization of laboratory equipment and surfaces. Its ability to degrade proteins makes it effective in removing proteinaceous material that may harbor contaminants.
Proteinase K is commercially available as a purified enzyme and is commonly used in various research applications, including DNA and RNA isolation, protein analysis, and molecular cloning. It is important to note that Proteinase K is highly stable and active over a wide range of pH and temperature conditions, which contributes to its versatility and utility in different experimental setups.
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