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- Product Information
- Products Characteristics
- Protocol & Manual
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- Quality & Safety
PROTEINASE K Molecular Biology Grade from Parengyodontium album (Tritirachium album) is a subtilisin-related serine protease
This recombinant enzyme is expressed in Pichia pastoris, and undergoes extensive purification to yield the highest quality product.
- Recombinant broad-spectrum non-specific protease derived from Tritirachium album and over-expressed in Pichia pastoris.
- High activity and exceptional purity .
- Active at high temperatures (up to 56°C) and denaturing conditions (e.g. in the presence of urea and/or SDS), what makes it ideal for digesting proteins in 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 powder, lyophilized “cake” or liquid.
- Extraction of DNA and RNA from different starting materials.
- Purification of target material from contaminating proteins.
- Removal of DNases and RNases during nucleic acids isolation.
One unit of Proteinase K hydrolyzes urea-denaturated hemoglobin producing color equivalent of 1 μmol tyrosine per 1 min at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.
Blirt’s Proteinase K MBG is interchangeable with comparators without dose adjustments.
Declared activity for all shown suppliers is ≥30 U/mg (blue line).
Proteinase K MBG activity after up to 2 years storage at -20°C is guaranteed by Certificate of Analysis, additionally performed experiments revealed only <14% activity loss after 3 years storage at -20°C (and it is still above-declared ≥30U/mg). It is a very important feature for molecular biology kits manufacturers.
Proteinase K MBG Solution storage at -20°C is recommended.
No significant differences in protein activity at +37°C after 18 months have been proven.
Proteinase K remains full activity in spite of temporary exposures to temperature changes e.g. during transportation or experiments.
Automation of the Proteinase K MBG Production results in minimal batch to batch activity variation.
Consistency in the product characteristics in all delivered batches guarantees reliable experiments results and stable working conditions.
Blue line represents declared minimum activity (≥ 30 U/mg). Batch-to-batch variation is 3,0% (with measurement error ± 1-6%).
PROTEINASE K Molecular Biology Grade - Description (powder)
PROTEINASE K Molecular Biology Grade - Description (solution)
PROTEINASE K Molecular Biology Grade - Flyer (Chinese)
Proteinase K MB Grade – Lyophilized powder
- Solubility in water
≥ 20 mg/ml
≥ 30 U/mg lyophilizate
≥ 40 U/mg protein
- Protein content
≥ 70% Protein content is determined by measuring absorbance at 280 nm.
- DNA content
≤ 10 pg/mg by qPCR
Proteinase K MB Grade – Solution
- Proteinase K concentration
≥ 800 U/ml
- DNA content
≤ 0.25 pg/U by qPCR
PROTEINASE K Molecular Biology Grade - MSDS - Powder
PROTEINASE K Molecular Biology Grade - MSDS - Solution
PROTEINASE K Molecular Biology Grade - Powder CoA L:NAE886174
PROTEINASE K Molecular Biology Grade - Powder CoA L:NAE855875
PROTEINASE K Molecular Biology Grade - Powder CoA L:NAE795775
PROTEINASE K Molecular Biology Grade - Powder CoA L:NAE566073
PROTEINASE K Molecular Biology Grade - Powder CoA L:876174
PROTEINASE K Molecular Biology Grade - Solution CoA L:NBE575875-F1
PROTEINASE K Molecular Biology Grade - Solution CoA L:NBE795775-F1
PROTEINASE K Molecular Biology Grade - Cake CoA L:736473-C1
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Influence of active compounds on the degradation of polylactide biocomposites
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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