RPROTK-RO
Roche
Proteinase K, recombinant, PCR Grade
Lyophilizate from Pichia pastoris
About This Item
Doporučené produkty
Quality Level
form
lyophilized
specific activity
~2 units/mg protein
packaging
pkg of 100 mg (03115879001)
pkg of 25 mg (03115836001)
pkg of 2 × 250 mg (03115801001)
pkg of 4 × 250 mg (03115852001)
manufacturer/tradename
Roche
pH range
4.0-12.5
storage temp.
2-8°C
General description
- Inhibitors: The enzyme is inactivated by Pefabloc® SC. However, it is not inactivated by metal ions, chelating agents (e.g., EDTA), sulfhydryl reagents, or trypsin and chymotrypsin inhibitors.
- Activators: Proteinase K activity is stimulated by the presence of denaturing agents (SDS and urea).
- pH Optimum: Proteinase K is stable over a wide pH range (4 – 12.5). The enzyme maintains full activity for several hours when incubated at a pH between 6.5 and 9.5.
- Volume Activity:
Approximately 30 U/mg lyophilizate (hemoglobin assay)
Note: SDS can increase the activity of Proteinase K as much as sevenfold.
Specificity
Application
- The enzyme is extremely effective on native proteins and can therefore be used to rapidly inactivate endogenous nucleases such as RNases and DNases during nucleic acid isolation. This property makes Proteinase K particularly suitable for the isolation of native RNA and DNA from tissues or cell lines.
- The enzyme promotes cell lysis by activating a bacterial autolytic factor.
- Proteinase K is used for the analysis of membrane structures by modifying proteins and glycoproteins on cell surfaces.
- Because the enzyme is tested for the absence of RNases and DNases, and is virtually free of DNA, it is especially suitable for isolating PCR and RT-PCR templates.
- Proteinase K can also be used to remove cellular debris during the preparation of colony lifts, and to treat tissue sections to ensure efficient probe infiltration during in situ hybridization.
Features and Benefits
- Choose an effective tool for template preparation. Inactivate DNases and RNases of most species.
- Count on consistent quality and performance. Stringent quality testing ensures optimal stability and high-level lot-to-lot performance.
- Prepare samples over a wide range of conditions. The robust enzyme is stable over a wide pH range and is ideal for diverse applications.
- Benefit from a contamination-free enzyme. The enzyme is tested for the absence of RNases and DNases, and is virtually free of DNA. It is especially suited for the isolation of PCR templates.
Note: The enzyme can reduce protein to free amino acids if it is present in large excess for long incubation periods.
Contents
Lyophilizate PCR Grade Proteinase K is also available in solution.
Quality
- Absence of Nucleases: Each lot is tested on various substrates to ensure the absence of endonuclease, exonuclease, ribonuclease and nicking activity.
- DNA content: =10 pg/mg enzyme (determined by Threshold)
- Bioburden: <125 cfu/g (determined by the most stringent test from the European Pharmacopoeia, which identifies the total number of viable aerobic bacteria, yeast, and fungi)
Preparation Note
Working solution: For best results, dissolve Proteinase K, recombinant, PCR Grade, in double-distilled water or Tris buffer. The best buffer for proteinase K will vary from application to application. Always follow the pH and temperature guidelines in parameter field. As a general rule, proteinase K is stable and very active in buffers that contain denaturing reagents such as urea, sodium dodecyl sulfate (SDS), and guanidinium salts.
Storage conditions (working solution): -15 to -25 °C
Reconstitution
Other Notes
Lyophilizate PCR Grade Proteinase K is also available in solution.
Legal Information
related product
signalword
Danger
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
does not flash
flash_point_c
does not flash
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