Our website will be undergoing scheduled maintenance and unavailable from Friday, January 20th at 2pm PT to Saturday, January 21st at 12am PT. We apologize for the inconvenience.
Quick Order
Welcome, Guest
About Affymetrix


Email | Print
Bookmark and Share

Proteinase K  

Highly active and stable endopeptidase purified from the fungus T. album

Part # Description Unit Size Your Price (USD)
76230Y 100 MG
Proteinase K
100 mg    $102.00
76230Z 500 MG
Proteinase K
This pack size will be discontinued as of 1/20/2017
500 mg    $468.00
76230 2X500 MG
Proteinase K
1 gm (2 x 500 mg)    $629.00
Bulk quantity and Custom requests  


Tritirachium album

Proteinase K is a highly active and stable endopeptidase used in a wide range of applications purified from the fungus T. album. It cleaves peptide bonds mainly following the carboxyl group of N-substituted hydrophobic aliphatic and aromatic amino acids(1) and is classified as a serine protease. Proteinase K is useful in purifying high molecular weight nucleic acids from cells and tissues (i.e. genomic DNA isolation from mouse tails) and in revealing protein structure and function.



Back to Top >

Molecular Weight: 28.9 kDa
Optimum pH: 4.0-12.5(1)
Optimum Temperature: 65°C(1)
Working Concentration: 0.05 - 1 mg/ml
Activators: Stimulated by 0.2 - 1% SDS or 1 - 4M urea(8)
Inactivated by PMSF(1); Not inactivated by EGTA, thiol reagents or trypsin/chymotrypsin inhibitors(1)

Lyophilized powder

Tested for contaminating ribonucleases and deoxyribonucleases.

Unit Definition:
One unit is the amount of enzyme that liberates folin positive amino acids and peptides corresponding to 1 μmol tyrosine in 1 min at 37°C using hemoglobin as substrate.

20 - 50 units/mg


  1. EBELING, W., HENNRICH, N., KLOCKOW, M., METZ, H., ORTH, H. D. AND LANG, H. (1974) Eur. J. Biochem. 47, 91-97.
  2. GROSS-BELLARD, M., OUDET, P. AND CHAMBON, P. (1973) Eur. J. Biochem. 36, 32-38.
  3. HANSEN, J. N. (1974) Prep. Biochem. 4, 473-488.
  4. KASCHE, V., ZOLLNER, R., AMNEUS, H. AND NASLUND, L. (1981) Prep. Biochem. 11, 233-250.
  5. ROELCKE, D. AND ULENBRUCK, G. (1969) Z. Med. Mikrobiot. und Immunol. 155, 156-170.
  6. BRDICZKA, D. AND KREBS, W.(1973) Biochem. Biophys. Acta 297, 203-212.
  7. WILLIAMSON, J., GREENE, J., CHERIF, S. AND MILNER-WHITE, E. J. (1977) Biochem. J. 167, 731-737.
  8. HILZ, H., WIEGERS, U. AND ADAMIETZ, P. (1975) Eur. J. Biochem. 56, 103-108.
  9. CROWE, J. S., COOPER, H., SMITH, M., SIMS, M., PARKER, D. AND GEWERT, D. (1991) Nucl. Acids. Res. 19, 184.


  1. Used in the isolation of native, high molecular weight DNA and RNA.
  2. Used as a general protease to inactivate DNases, RNases and to degrade proteins.
  3. Specifically modifies cell surface proteins and glycoproteins for analysis of membrane structures for protein localization(5,6).
  4. Produces characteristic protein fragments used in enzyme/protein structure and function studies(7).


Shipped on cold pack. Store dry at 4°C.

Back to Top >

MSDS / Material Safety Data Sheets

Proteinase K SDS

Back to Top >

Currently there are no required/related products displayed for this product.

Back to Top >