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Proteinase K from Parengyodontium album (Tritirachium album) is a subtilisin-related serine protease. It is a broad-spectrum endopeptidase with a very high specific activity. It is widely used for the digestion of proteins, including DNases and RNases, during nucleic acid preparations without compromising the integrity of isolated DNA or RNA. Proteinase K is active under a wide range of reaction conditions, including elevated temperatures and the presence of SDS. This recombinant enzyme is expressed in Pichia pastoris, and undergoes extensive purification to yield the highest quality product. An extra purification step results in significantly increased solubility (2.5 fold), increased specific activity, and decreased DNA content, compared to our Molecular Biology Grade product.
Below, you can see the comparison of Proteinase K MBG and NGS Grade (Table 1 ).
- Recombinant broad-spectrum non-specific protease derived from Tritirachium album and over-expressed in Pichia pastoris.
- High activity and exceptional purity (Molecular Biology Grade & NGS Grade).
- Active at high temperatures (up to 56°C) and under denaturing conditions (e.g. in the presence of urea and/or SDS), which makes it ideal for digesting proteins in a variety of applications.
- Stable over a wide pH range: 4.0–12.5 (optimum pH 7.5–8.0).
- Decreased amount of host DNA (≤ 10 pg/mg / MBG or ≤ 0.1 pg/mg NGS).
- Available as a lyophilized powder.
- Extraction of DNA and RNA from different starting materials.
- Removal of DNases and RNases during nucleic acid isolation.
- Purification of samples contaminated with different protein
- Automated isolation stations
One unit of Proteinase K hydrolyzes urea-denaturated hemoglobin producing a color equivalent of 1 μmol tyrosine per 1 min at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.
Proteinase K – Lyophilized powder, NGS Grade
- DNA content
≤ 0.1 pg/mg by qPCR
- Solubility in water
≥ 50 mg/ml
≥ 35 U/mg lyophilizate
≥ 45 U/mg protein
- Protein content
≥ 70% Protein content is determined by measuring absorbance at 280 nm.
Proteinase K Stock solution preparation
- 20-50 mg/ml solutions: use purified water for immediate use; or 50% glycerol in purified water (v/v) for long-term storage at -20˚C.
- < 20 mg/ml solutions: use 50 mM Tris-HCl, pH = 7.8, 3 mM CaCl2 for immediate use; or 50 mM Tris-HCl, pH = 7.8, 3 mM CaCl2 , 50% glycerol for long-term storage at -20˚C.
Influence of active compounds on the degradation of polylactide biocomposites
Authors Magdalena Stepczyńska Products Proteinase K Year 2019 Source Polimery, 2019, Vol. 64 Issue 6, p410-416. 7p.
Enzymatic degradation of bacteriostatic polylactide composites
Authors Agnieszka Richert, Ewa Olewnik-Kruszkowska, Edyta Adamska, Iwona Tarach Products Proteinase K Year 2019 Source International Biodeterioration & Biodegradation, Volume 142, 2019, Pages 103-108
Broadening the tools for studying sand fly breeding habitats: A novel molecular approach for the detection of phlebotomine larval DNA in soil substrates
Authors I.A. Giantsis, A. Chaskopoulou, Products Proteinase K Year 2019 Source Acta Tropica, Volume 190, 2019, Pages 123-128
Enzymatic degradation of flax-fibers reinforced polylactide
Authors Magdalena Stepczyńska, Piotr Rytlewski Products Proteinase K Year 2018 Source Elsevier
Flax fibres reinforced polylactide modified by ionizing radiation
Authors Piotr Rytlewski, Magdalena Stepczyńska, Uwe Gohs, Rafał Malinowski, Bogusław Budner, Marian Żenkiewicz Products Proteinase K Year 2018 Source Elsevier
A comparative analysis of mass losses of some aliphatic polyesters upon enzymatic degradation
Authors Marian Żenkiewicz, Agnieszka Richert, Rafał Malinowski, Krzysztof Moraczewski Products Proteinase K Year 2012 Source Elsevier
Some composting and biodegradation effects of physically or chemically
Authors Marian Żenkiewicz, Rafał Malinowski, Piotr Rytlewski, Agnieszka Richert, Wanda Sikorska, Katarzyna Krasowska Products Proteinase K Year 2011 Source Elsevier