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Proteinase K(PCR Grade)  
                                 -------------Available in stock, bulk supply                      

Catalog #

Pack size


ZB117S 1g 150.00



70 000.00

       Proteinase K is a subtilisin-like endolytic protease that is isolated from the saprophytic fungus Tritirachium album. It has a high activity that is stable across a wide range of pH and temperature conditions and is suited to short digestion times. The activity of proteinase K is increased at elevated temperatures up to 65°C. Calcium is not essential to the function of proteinase K. Therefore, EDTA and other chelating agents do not interfere with the activity and may be used alongside proteinase K to inactivate calcium-dependent nucleases in DNA and RNA preparation.

Properties of Proteinase K

Alternate names

Peptidase K, Tritirachium alkaline proteinase


Cleaves at the carboxyl side of aliphatic, aromatic or hydrophobic residues

Proteinase K Source

Tritirachium album


White Lyophilized Powder

Molecular weight



Lyophilized form


>30 units/mg at 35°C


RNase-free and DNase-free

Protease type

Serine protease


Inactivation of RNase and DNase during nucleic acid purification

Reaction conditions

0.05-1 mg/ml proteinase K, pH 7.5-8, often containing 0.5-1% SDS

Storage conditions

Store at -20°C,shipped in RT



 Isolation of high molecular weight DNA
Isolation of plasmid and genomic DNA
Isolation of RNA
 Inactivation of RNase and DNase activities 

Storage buffer

20 mM Tris-HCl (pH 7.4), 1 mM CaCl2, 50 % Glycerol.
Quality control Unit definition
One unit is defined as the amount of enzyme that liberates folin-positive amino acids and peptides corresponding to 1 µmol tyrosine under the assay conditions in 1 minute using hemoglobin as substrate.
16-hour incubation
A 50 µl reaction containing 1 µg of λ DNA and 1.8 U of enzyme incubated for 16 hours at 37°C resulted in the same DNA band as that produced without the enzyme.
Exonuclease activity
Incubation of 6 U for 4 hours at 37°C in 50 µl assay buffer with 1 µg sonicated [3H]-DNA (2 x 105 cpm/µg) released <0.2 % of radioactivity.
Endonuclease activity
Incubation of 1.8 U with 1 µg φX174 RFI DNA (4 hours, 37°C, 50 µl) gave <5 % conversion to RFII.
RNase activity
Incubation of 6.0 U with 1 µg MS2 RNA (4 hours, 37°C, 50 µl) resulted in the same RNA band as that produced without the enzyme.
Common features
Proteinase K has two binding sites for Ca2+. Calcium acts as a stabilizing factor of the enzyme. When calcium is removed from the solution, the activity of proteinase K decreases slowly.

Proteinase K
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