Promega's Cookie Policy

We use cookies and similar technologies to make our website work, run analytics, improve our website, and show you personalized content and advertising. Some of these cookies are essential for our website to work. For others, we won’t set them unless you accept them. To find out more about cookies and how to manage cookies, read our Cookie Policy.

Our website does not fully support your browser.

We've detected that you are using an older version of Internet Explorer. Your commerce experience may be limited. Please update your browser to Internet Explorer 11 or above.

Proteinase K (Lyophilized)

For General Digestion of Protein in Biological Samples

  • Active over a pH range of 4.3–12.0, in 0.5% SDS or 1% Triton® X-100
  • Purified to remove RNase and DNase activities

Size

Catalog number selected: V3021

$ 139.00
Your price:
Please Enquire
This product is discontinued
Add to Helix
Proteinase K (Lyophilized)
100mg
$ 139.00
Your price: Log in

Produced by the fungus Tritirachium album Limber; is a serine protease with broad cleavage activity. Proteinase K cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples. It has been purified to remove RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparations of DNA and RNA. A typical working concentration for Proteinase K is 50–100μg/ml.

Form: Lyophilized powder.

Recommended Reaction Buffer: 50mM Tris-HCl (pH 8.0), 10mM CaCl2.

References
  1. Ebeling, W. et al. (1974) Eur. J. Biochem. 47, 91–7.
  2. Schwartz, D.C. and Cantor, C.R. (1984) Cell 37, 67–75.
  3. Cleveland, D.W. et al. (1977) J. Biol. Chem. 252, 1102–6.
  4. Hames, B.D. (1981) In: Gel Electrophoresis of Proteins: A Practical Approach, B.D. Hames and D. Rickwood, eds., IRL Press, Oxford, 219.
  5. Herrmann, B.G. and Frischauf, A.M. (1987) Meth. Enzymol. 152, 180–3.
  6. Lee, J.J. and Costlow, N.A. (1987) Meth. Enzymol. 152, 633–48.
  7. Sambrook, J. et al. (1989) Molecular Cloning: A Laboratory Manual, Vol. 3, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  8. Sweeney, P.J. and Walker, J.M. (1993) Enzymes of molecular biology. In: Methods in Molecular Biology, Vol. 16, M.M. Burrell, ed., Humana Press, Inc., Totowa, NJ, 305.

Specifications

What's in the box?

Item Part # Size

Proteinase K

V302B 1 × 100mg

SDS

Choose language:

Certificate of Analysis

Search by lot number

Use Restrictions

For Research Use Only. Not for Use in Diagnostic Procedures.

Storage Conditions

BB

Let's find the product that meets your needs.

Talk to a Scientist

Maria

Maria

Spain