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| Name | Proteinase K, recombinant |
| Source | Recombinant |
| Enzyme Type | Protease |
| Molecular Weight | 28.9 kDa |
| Optimal PH | 7.5-8.0 |
| Optimal Temperature | 37°C |
| Storage Temperature | -20°C |
| Specific Activity | ≥30 units/mg |
| Purity | ≥98% |
| Form | Lyophilized powder |
| Applications | DNA and RNA isolation, protein purification, removal of nucleases |
| Product Size | 500 mg |
| Catalog Number | P8107 |
FAQ
What is Proteinase K and what is its role in molecular biology research?
Proteinase K is a recombinant enzyme that is commonly used in molecular biology research to digest proteins in samples such as tissues, cells, and nucleic acid preparations. This enzyme is highly stable and active over a wide range of conditions, making it an essential tool for researchers working with DNA and RNA.
How does Proteinase K work and what are its specific applications in the laboratory?
Proteinase K works by cleaving peptide bonds in proteins, resulting in their degradation. This enzyme is particularly useful in purifying nucleic acids from biological samples, as it can efficiently remove proteins that may interfere with downstream applications such as PCR, sequencing, and cloning. Proteinase K is also employed in various protocols for isolating and analyzing proteins, as well as in studies of gene expression and regulation.
What are the key features of recombinant Proteinase K that make it a preferred choice for molecular biology experiments?
Recombinant Proteinase K offers several advantages over traditional Proteinase K sourced from native organisms. Its recombinant nature ensures batch-to-batch consistency and high purity, minimizing the risk of contamination of samples. Moreover, recombinant Proteinase K is free from any contaminating nucleases or other proteases that could degrade nucleic acids, making it a reliable and robust enzyme for sensitive molecular biology applications.
How should Proteinase K be stored and handled to maintain its stability and activity?
Proteinase K should be stored at -20°C in a non-frost-free freezer to maintain its stability over time. Before use, the enzyme should be thawed on ice and aliquoted to prevent repeated freeze-thaw cycles, which can decrease its activity. Additionally, Proteinase K should be handled with care to avoid contamination and exposure to other proteins, enzymes, or nucleic acids that could compromise its performance in experiments.
What are some troubleshooting tips for working with Proteinase K in molecular biology experiments?
If Proteinase K fails to digest proteins efficiently in a sample, several factors should be considered to troubleshoot the issue. First, ensure that the enzyme is active by testing its performance in a control reaction. If necessary, increase the concentration or incubation time of Proteinase K to enhance its activity. Additionally, verify that the buffer conditions and temperature are optimal for Proteinase K digestion, as these factors can affect the enzyme's efficiency. Finally, check for any inhibitors or contaminants in the sample that may be interfering with Proteinase K activity and adjust the experimental conditions accordingly.
Proteinase K is a recombinant enzyme that is commonly used in molecular biology research to digest proteins in samples such as tissues, cells, and nucleic acid preparations. This enzyme is highly stable and active over a wide range of conditions, making it an essential tool for researchers working with DNA and RNA.
How does Proteinase K work and what are its specific applications in the laboratory?
Proteinase K works by cleaving peptide bonds in proteins, resulting in their degradation. This enzyme is particularly useful in purifying nucleic acids from biological samples, as it can efficiently remove proteins that may interfere with downstream applications such as PCR, sequencing, and cloning. Proteinase K is also employed in various protocols for isolating and analyzing proteins, as well as in studies of gene expression and regulation.
What are the key features of recombinant Proteinase K that make it a preferred choice for molecular biology experiments?
Recombinant Proteinase K offers several advantages over traditional Proteinase K sourced from native organisms. Its recombinant nature ensures batch-to-batch consistency and high purity, minimizing the risk of contamination of samples. Moreover, recombinant Proteinase K is free from any contaminating nucleases or other proteases that could degrade nucleic acids, making it a reliable and robust enzyme for sensitive molecular biology applications.
How should Proteinase K be stored and handled to maintain its stability and activity?
Proteinase K should be stored at -20°C in a non-frost-free freezer to maintain its stability over time. Before use, the enzyme should be thawed on ice and aliquoted to prevent repeated freeze-thaw cycles, which can decrease its activity. Additionally, Proteinase K should be handled with care to avoid contamination and exposure to other proteins, enzymes, or nucleic acids that could compromise its performance in experiments.
What are some troubleshooting tips for working with Proteinase K in molecular biology experiments?
If Proteinase K fails to digest proteins efficiently in a sample, several factors should be considered to troubleshoot the issue. First, ensure that the enzyme is active by testing its performance in a control reaction. If necessary, increase the concentration or incubation time of Proteinase K to enhance its activity. Additionally, verify that the buffer conditions and temperature are optimal for Proteinase K digestion, as these factors can affect the enzyme's efficiency. Finally, check for any inhibitors or contaminants in the sample that may be interfering with Proteinase K activity and adjust the experimental conditions accordingly.
