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Name | Proteinase K - Solution |
Type | Enzyme |
Source | Genetically modified Pichia pastoris |
Concentration | 20 mg/ml |
Storage Conditions | Store at -20°C |
Activity | Broad spectrum serine protease |
Specificity | Cleaves proteins specifically at the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids |
Applications | DNA and RNA extraction, protein purification, tissue dissociation |
Molecular Weight | ≈ 29.5 kDa |
Optimal PH | 7.5-8.5 |
Optimal Temperature | 50-60°C |
Unit Definition | One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per minute at pH 7.5 at 37ºC |
Form | Liquid |
Solubility | Soluble in water |
FAQ
What is Proteinase K and how is it used in research applications?
Proteinase K is a highly active and stable endopeptidase that cleaves peptide bonds adjacent to the carboxylic group of aliphatic or aromatic amino acids. It is commonly used in molecular biology applications to digest unwanted proteins or to inactivate nucleases that may be present in a sample. Proteinase K is particularly useful in DNA and RNA extraction protocols, where it effectively degrades proteins without affecting nucleic acids.
How does Proteinase K work?
Proteinase K works by hydrolyzing peptide bonds in proteins, resulting in their breakdown into smaller peptides or amino acids. This enzyme is active under a wide range of conditions, including high temperatures and in the presence of denaturing agents such as SDS. Its broad specificity allows it to efficiently cleave most proteins, making it a versatile tool in various research applications.
What are the benefits of using Proteinase K in research experiments?
Proteinase K offers several key advantages for researchers. It is highly active and can effectively remove proteins from samples without compromising the integrity of nucleic acids. Additionally, Proteinase K is stable and retains its activity in a wide range of experimental conditions, making it a reliable enzyme for various applications. Its broad specificity also ensures that it can target a wide range of proteins, providing researchers with a versatile tool for protein digestion.
How should Proteinase K be stored and handled to ensure its stability and effectiveness?
Proteinase K should be stored in a cool, dry place at -20°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles, as this can lead to a decrease in enzymatic activity. When handling Proteinase K, it is recommended to use nuclease-free buffers and equipment to prevent contamination and preserve its activity. Additionally, care should be taken to protect the enzyme from exposure to nucleases, which can degrade its activity over time.
In what research applications is Proteinase K commonly used?
Proteinase K is widely used in molecular biology and biochemistry research for various applications. Some common uses of Proteinase K include DNA and RNA extraction, protein digestion for mass spectrometry analysis, and removal of proteins from tissue samples. This enzyme is also employed in the study of protein-protein interactions, cell signaling pathways, and protein structure analysis. Its versatility and reliability make Proteinase K a valuable tool for researchers in diverse fields.
Proteinase K is a highly active and stable endopeptidase that cleaves peptide bonds adjacent to the carboxylic group of aliphatic or aromatic amino acids. It is commonly used in molecular biology applications to digest unwanted proteins or to inactivate nucleases that may be present in a sample. Proteinase K is particularly useful in DNA and RNA extraction protocols, where it effectively degrades proteins without affecting nucleic acids.
How does Proteinase K work?
Proteinase K works by hydrolyzing peptide bonds in proteins, resulting in their breakdown into smaller peptides or amino acids. This enzyme is active under a wide range of conditions, including high temperatures and in the presence of denaturing agents such as SDS. Its broad specificity allows it to efficiently cleave most proteins, making it a versatile tool in various research applications.
What are the benefits of using Proteinase K in research experiments?
Proteinase K offers several key advantages for researchers. It is highly active and can effectively remove proteins from samples without compromising the integrity of nucleic acids. Additionally, Proteinase K is stable and retains its activity in a wide range of experimental conditions, making it a reliable enzyme for various applications. Its broad specificity also ensures that it can target a wide range of proteins, providing researchers with a versatile tool for protein digestion.
How should Proteinase K be stored and handled to ensure its stability and effectiveness?
Proteinase K should be stored in a cool, dry place at -20°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles, as this can lead to a decrease in enzymatic activity. When handling Proteinase K, it is recommended to use nuclease-free buffers and equipment to prevent contamination and preserve its activity. Additionally, care should be taken to protect the enzyme from exposure to nucleases, which can degrade its activity over time.
In what research applications is Proteinase K commonly used?
Proteinase K is widely used in molecular biology and biochemistry research for various applications. Some common uses of Proteinase K include DNA and RNA extraction, protein digestion for mass spectrometry analysis, and removal of proteins from tissue samples. This enzyme is also employed in the study of protein-protein interactions, cell signaling pathways, and protein structure analysis. Its versatility and reliability make Proteinase K a valuable tool for researchers in diverse fields.