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P8044

Sigma-Aldrich

Proteinase K from Tritirachium album

≥3.0 unit/mg solid, lyophilized powder

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Synonym(s):
Endopeptidase K
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

biological source

maize
microbial (T.album
T. ALBUM)

plant seeds (barley)
soybean
yeast

Quality Level

form

lyophilized powder

specific activity

≥3.0 unit/mg solid

mol wt

28.93 kDa

composition

Protein, ≥15% biuret

technique(s)

DNA extraction: suitable

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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1 of 4

This Item
SRE0047P6556SRE0005
biological source

maize, plant seeds (barley), yeast, microbial (T.album
T. ALBUM), soybean

biological source

fungus (Tritirachium album)

biological source

-

biological source

-

technique(s)

DNA extraction: suitable

technique(s)

-

technique(s)

DNA extraction: suitable

technique(s)

-

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

diagnostic assay manufacturing

Quality Level

200

Quality Level

400

Quality Level

300

Quality Level

500

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

Application

Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. It is used for the removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A. It is also useful for the isolation of hepatic, yeast, and mung bean mitochondria and is used to determine enzyme localization on membranes. Furthermore, it is used for the treatment of paraffin embedded tissue sections to expose antigen binding sites and for digestion of proteins from brain tissue samples. Product P8044 is provided as a lyophilized powder.
The enzyme from Sigma has been used to degrade complex I (NADH:ubiquinone oxidoreductase) prior to extraction of ubiquinone from Yarrowia lipolytica. It has been used to examine the effect of Proteinase k on Pythium ultimum. It has also been used to maximize the variety of peptide bonds hydrolyzed in the sediment slurry without autolytic production of amino acids from the enzyme itself.
Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.
Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria
Determination of enzyme localization on membranes
Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.
Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

Biochem/physiol Actions

Proteinase K is highly active towards native proteins. It has a broad specificity and degrades many proteins even in the native state. It mainly cleaves the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked α-amino groups. The optimum pH is between 7.5-9.0 and the isoelectric point is 8.9. Ca2+ (1-5 mM) is required for activation. Proteinase K is inhibited by diisopropyl fluorophosphate (DFIP), and phenylmethanesulfonyl fluoride (PMSF).
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

Unit Definition

One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Articles

Proteinase K is commonly used in molecular biology and biochemistry applications to digest structural proteins and enzymes. It is useful in removing nucleases that can degrade DNA and RNA, as well as in the isolation of intact genomic DNA from various sources.

The use of Pro K in combination with other reagents, such as detergents and chaotropic agents, can help to disrupt the cell membranes and release DNA from tissue. This is particularly important for downstream applications such as PCR, sequencing, and other molecular biology techniques that require pure and intact DNA.

The cost of proteinase K can vary depending on the source, purity, manufacturing process and vendor’s quality management system. It is important to balance the cost with the desired quality, performance, documentation and technical/quality support to select the optimal Proteinase K for the intended application

In blood DNA extraction, Proteinase K, an enzyme commonly used to degrade proteins, can help break down the cellular and nuclear membranes, releasing DNA from the cells that protect it from degradation and increase purity/yield making it more suitable for various molecular biology techniques.

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Protocols

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

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