Grade
Molecular Biology Grade
Description
Proteinase K is a recombinant enzyme that expressed in Pichia pastoris which is originally isolated from the mold Tritirachium album. It is highly active, subtilisin-related serine endopeptidases that does not exhibit any pronounced cleavage specificity. Thus, Proteinase K is treated as a universal tool for nucleic acid template preparation.
The recombinant form and native protease are having identical amino acid sequence and molecular structure. Compared to native protease, the recombinant enzyme guarantees an enzyme of outstanding reliability and purity meeting all requirements of molecular and diagnostic tests. The recombinant form of Proteinase K enzyme maximizes the yield of target nucleic acids. The lyophilized form as well as the solution form experience stability at room temperature and flexibility during shipment at room temperature.
Applications
- Digest native proteins very efficiently.
- Inactivate endogenous RNases and DNases rapidly during nucleic acid isolation.
- Isolation of native RNA and DNA from tissues and cell lines.
- Promotes cell lysis by activating a bacterial autolytic factor.
- Analysis of membrane structures by modifying proteins and glycoproteins on cell surfaces.
- Removal of cellular debris during the preparation of colony lifts.
- Treatment of tissue sections to ensure efficient probe infiltration during in situ hydridization.
Unit Definition of Protenaise K (lyophilized form)
Approximately 50U/ml solution (chromozyme assay); approximately 600U/ml solution (hemoglobin assay). One unit is the enzyme activity which cleaves at 25°C in 1 min 18mmol Chromozym TRY (equivalent to 600U/ml with the hemoglobin assay).
Specification of Proteinase K (lyophilized form)
| Assay | Result |
| Activity (37°C, with hemoglobin) | 43U/mgP |
| Activity (25°C, with chromozyme) | 2.8U/mgL |
| Specific activity (25°C, with chromozyme) | 3.24U/mgP |
| Optimum pH | 6.5 and 9.5 |
| pH range | 4.0 – 12.5 |
| Endonuclease up to 200mcg w.MWM III-DNA | Not detectable. |
| DNase up to 200mcg enzyme with pBR322-DNA | Not detectable. |
| RNase up to 40mcg enzyme with MS 2-RNA | Not detectable. |
| DNA (threshold) | 5pg/mg |
| Bioburden | <13 CFU/g |
Specification of Proteinase K (solution form)
| Assay | Result |
| Protein (biuret) | 20 mg/ml |
| Activity (37°C, with hemoglobin) | 862 U/ml |
| Specific activity (37°C, with hemoglobin) | 48 U/mg |
| Activity (25°C, with chromozyme) | 68 U/ml |
| Specific activity (25°C, with chromozyme) | 3.76 U/mg |
| Optimum pH | 6.5 and 9.5 |
| pH range | 4.0 – 12.5 |
| Endonuclease up to 200mcg w.MWM III-DNA | Not detectable. |
| DNase up to 200mcg enzyme with pBR322-DNA | Not detectable. |
| RNase up to 40mcg enzyme with MS 2-RNA | Not detectable. |
| DNA (threshold) | 0 pg/mg |
| Bioburden | <1 CFU/ml |
Storage
Store at -20°C for long shelf life
Store at 4°C and ambient temperature for short shelf life up to 1 year
Ordering Information
| Catalog No | Description | Pack Size |
| PC0712-100mg | Proteinase K | 100mg |
| PC0712 - 1g | Proteinase K | 1g |
| PC0712 - 1ml | Proteinase K | 1ml |
Download
Manual
Proteinase K (lyophilized form)
Proteinase K (solution form)
Download
MSDS
Publication
This Product Has Been Used In:
Watanapokasin, R., Imoto, M., Innajak, S., Kritsanawong, S. (2016). Antiproliferative and apoptosis induction of α-mangostin in T47D breast cancer cells, International Journal of Oncology, Vol. 48, No. 5 (2016).
Rahman, R.A., Sukri, N.M., Nazir, N.M., Aa’zamuddin, M., Radzi, A., Zulkifly, A.H., Ahmad, A.C., Hashi, A.A., Rahman, S.A., Sha’ban, M. (2015). The potential of 3-dimensional construct engineered from poly(lactic-co-glycolic acid)/fibrin hybrid scaffold seeded with bone marrow mesenchymal stem cells for in vitro cartilage tissue engineering. Tissue and Cell 47 (4). Pp.420-430
Abdel-Gawad, F.K. et al. (2014) Carboxymethyl Chitosan Modulates the Genotoxic Risk and Oxidative Stress of Perfluorooctanoic Acid in Nile Tilapia (Oreochromis niloticus). Journal of the Saudi Society of Agricultural Sciences.ScienceDirect.
Fadavi, P., Rostamian, M., Arashkia, A., Shafaghi, B., Niknam, H.M. (2013). Epstein-barr virus may not be associated with breast cancer in Iranian patients, Oncology Discovery, (2013).
