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Proteinase K(PCR Grade)
-------------Available in stock, bulk supply
Catalog # |
Pack size |
Price($) |
|
ZB117S |
1g |
150.00
|
ZB117L |
1Kg |
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
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Alternate names |
Peptidase K,
Tritirachium alkaline proteinase |
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Specificity
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Cleaves at the
carboxyl side of aliphatic, aromatic or hydrophobic
residues |
|
Proteinase K Source
|
Tritirachium
album |
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Appearance
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White
Lyophilized Powder |
|
Molecular weight
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28,900
|
|
Form
|
Lyophilized
form |
|
Concentration/activity |
>30 units/mg
at 35°C |
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RNase/DNase
|
RNase-free and
DNase-free |
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Protease type
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Serine
protease |
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Uses/applications
|
Inactivation
of RNase and DNase during nucleic acid purification
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Reaction conditions
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0.05-1 mg/ml
proteinase K, pH 7.5-8, often containing 0.5-1% SDS
|
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Storage conditions
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Store at -20°C,shipped
in RT |
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Inhibitors
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PMSF or DFP
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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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