Proteinase K

*This product has been discontinued!*

Protease K is a subtilian-type protease isolated from the saprophytic fugus Tritirachim album. It is particularly suitable for short digestions. It possesses a very broad peptide cleavage activity, which remains stable over a wide range of temperatures and pH values, although its activity increases at higher temperature.

Cat. No.	Z02003
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Product Introduction Applications

Description

Protease K is a subtilian-type protease isolated from the saprophytic fugus Tritirachium album. It is particularly suitable for short digestions. It possesses a very broad peptide cleavage activity, which remains stable over a wide range of temperatures and pH values, although its activity increases at higher temperature.

Synonyms

Proteinase K;

Note

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Product Introduction

Source	Tritirachium album
Biological Activity	>30 units/mg protein (hemoglobin, pH7.5, 37^oC) Unit Definition: It is the amount of enzyme which releases at 37 ^oC in 1 min as many folin-positive amino acid and peptides from hemoglobin as 1umol of tyrosine.
Reconstitution	Reconstitute lyophilized Proteinase K in ddH2O at 1 mg/ml and yield a clear colorless solution.
QC	Purified by chromatography RNases: Not detectable DNases: Not detectable Exonucleases: Not detectable
Usage	In presence of 0.5-1.0% SDS, Proteinase K inactivates DNases and RNases in eukaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of intact highly-molecular nucleic acids.
Storage & Stability	Lyophilized recombinant Proteinase K remains stable up to 3 years at -20°C. Upon reconstitution, Proteinase K should be stable up to 1 year at -20°C.
Key Features	Proteinase K is a highly active and stable protease with low cutting specificity. The enzyme belongs to the group of subtilisine-related serine proteases and is strongly inhibited by PMSF.

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Applications

See datasheet for details.

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