Proteinase K Solution – 5ml
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Proteinase K Solution – 5ml

  • $81.02 Model Number IB05406
  • Save $43


  • Concentration: 20mg/ml
  • Used for digestion of the protein keratin

IBI’s Proteinase K Solution is a stable 20 mg/ml highly active proteolytic enzyme that is purified from the mold Tritirachium album. The enzyme has two binding sites for Ca++, which lie some distance from the active site and are not directly involved in the catalytic mechanism. The high activity of the enzyme solution (0.6 U/µl) means that you can keep the reaction volumes low (as low as 200 µg/ml). It also means that you can expect more complete digestion of your samples. Proteinase k solution is used to digest proteins and remove contaminants from nucleic acid sample preparations that can degrade DNA and RNA during purification. It is ideal for this application since the enzyme is active in the presence of chemicals that denture proteins such as SDS and urea.

Example: For a final concentration of 200 µg/ml, add 1 ml of Proteinase K solution to your sample.

Physical Specifications
CAS#: N/A
Tris: 10 mM
Calcium Chloride: 1 mM
Glycerol: 30%
pH: Adjusted to 8.0 with HCl.

Molecular Biology Specifications
DNase Assay (Endo and Exo): None Detected
RNase Assay: None Detected
Protease Activity on Gel Substrate: Pass

IB05406 - Specification Sheet

Recommended Use
IBI’s Proteinase K Solution is a stable 20mg/ml highly active proteolytic enzyme that is purified from the mold Tritirachium album.
The enzyme has two binding sites for Ca++, which lie some distance from the active site and is not directly involved in the catalytic mechanism.
The high activity of the enzyme solution (0.6 U/μl) means that you can keep the reaction volumes low, as low as 200 mg/mL.
It also means that you can expect more complete digestion of your samples. Example: For a final concentration of 200 μg/ml, add 1 ml of Proteinase K Solution to your sample.

Storage
Store at +4°C.

How do I deactivate the Proteinase K in my sample? Heat the sample to 95° C for 20-30 minutes.