Proteinase K

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Proteinase K P-1265
  • CAS: 39450-01-6
  • MW: 28,500 Da
  • Appearance: White to off-white lyophilized solid

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Proteinase K is a nonspecific serine protease used in the following applications: inactivation of Rnase and Dnases, isolation of high molecular weight DNA, isolation of RNA or the isolation of plasmid and genomic DNA. Proteinase K is used for the isolation of native high molecular genomic nucleic acids. Enzymes like DNases and RNases from microorganisms and mammalian cells are rapidly inactivated by Proteinase K.

Adding Proteinase K already during the cell lysis enables the isolation of highly native undamaged high molecular DNA or RNA. A variety of methods have been established, which are documented in numerous publications. Recently, Proteinase K has been used for the detection of BSE forming proteins which are uniquely resistant towards the enzyme's proteolytic cleavage.

Proteinase K is very useful in the analysis of membrane structure by means of modification of proteins and glycoproteins on cell surfaces. Because of the cleavage specificity Proteinase K, characteristic fragments of proteins are obtained which are helpful in revealing the structure and function of proteins, particularly enzymes.

Additional Information

Product # P-1265
CAS # 39450-01-6
MW 28,500 Da
Appearance White to off-white lyophilized solid
Solubility 50mM Tris-HCl, 2mM calcium acetate, pH 8.0
Storage Temp Store desiccated at +4°C. Store in tightly sealed vial.
Use Proteinase K is a stable and highly reactive serine protease

Additional Information

MDL Number MFCD00132129

Additional Information

GHS Pictograms
Handling Store desiccated at +4°C. Store in tightly sealed vial.
Hazard Image Yes

Additional Information

msds 1 P-1265, SDS.pdf
Certificate of Analysis 1 P-1265, H1281.pdf
Certificate of Analysis 2 P-1265, H1069D.pdf
Certificate of Analysis 3 P-1265, H1069C.pdf

Additional Information

Reference Site-specific O-Glycosylation Analysis of Human Blood Plasma Proteins - S\nMarcus Hoffmann, Kristina Marx, Udo Reichl, Manfred Wuhrer, and Erdmann Rapp.
Evaluation of two novel leptospiral proteins for their interaction with human host components - Lucas P. Silva Luis G. V. Fernandes Monica L. Vieira Gisele O. de Souza Marcos B. Heinemann Silvio A. Vasconcellos Eliete C. Romero Ana L. T. O. Nascimento
Identification of new molecular alterations in fatal familial insomnia - Franc Llorens, Katrin Thune, Matthias Schmitz, Belen Ansoleaga, Margalida A. Frau-Mendez, Maria Cramm, Waqas Tahir, Nadine Gotzmann, Sara Berjaoui, Margarita Carmona, Christopher J. Silva, Ivan Fernandez-Vega, Juan Jose Zarranz, Inga Zerr, and Isidro Ferrer.
Glucocerebrosidase modulates cognitive and motor activities in murine models of Parkinson’s disease - Edward Rockenstein, Jennifer Clarke, Catherine Viel, Nicholas Panarello, Christopher M. Treleaven, Changyoun Kim, Brian Spencer, Anthony Adame, Hyejung Park, James C. Dodge, Seng H. Cheng, Lamya S. Shihabuddin, E. Masliah, and S. Pablo Sardi.
Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant α-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson’s disease - Mari Suzuki, Nobuhiro Fujikake, Toshihide Takeuchi, Ayako Kohyama-Koganeya, Kazuki Nakajima, Yoshio Hirabayashi, Keiji Wada and Yoshitaka Nagai.

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