Proteinase K

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Proteinase K P-1265
  • CAS: 39450-01-6
  • MW: 28,500
  • 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

SynonymsEndopeptidase K
Product #P-1265
CAS #39450-01-6
AppearanceWhite to off-white lyophilized solid
Solubility50mM Tris-HCl, 2mM calcium acetate, pH 8.0
Storage TempStore desiccated at +4°C. Store in tightly sealed vial. WARNING: HARMFUL! IRRITANT!
UseProteinase K is a stable and highly reactive serine protease

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MDL NumberMFCD00132129

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GHS Pictograms
HandlingStore desiccated at +4°C. Store in tightly sealed vial.
Hazard ImageYes

Additional Information

msds 1P-1265, Proteinase K, SDS, diamond format.pdf
Certificate of Analysis 1P-1265, J1298.pdf
Certificate of Analysis 2P-1265, J1072I.pdf
Certificate of Analysis 3P-1265, J1072H.pdf
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CitationsLocalization and distribution of primary cilia in adult mouse heart
ReferenceSite-specific O-Glycosylation Analysis of Human Blood Plasma Proteins - Marcus 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 Parkinsons 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 alpha synuclein and aggravates neurodegeneration in a Drosophila model of Parkinsons disease Mari Suzuki, Nobuhiro Fujikake, Toshihide Takeuchi, Ayako Kohyama Koganeya, Kazuki Nakajima, Yoshio Hirabayashi, Keiji Wada and Yoshitaka Nagai.
Localization and distribution of primary cilia in adult mouse heart

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