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

Catalog #

Pack size

Price($)

ZB117S 1g 670.00

ZB117L

1Kg

100 000.00

       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

Specificity

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

Proteinase K Source

Tritirachium album

Appearance

White Lyophilized Powder

Molecular weight

28,900

Form

Lyophilized form

Concentration/activity

>30 units/mg at 35°C

RNase/DNase

RNase-free and DNase-free

Protease type

Serine protease

Uses/applications

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

Inhibitors

PMSF or DFP

 Applications
 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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