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70663

Millipore

Proteinase K, Lyophilized

Highly active serine protease that exhibits broad cleavage specificity on native and denatured proteins and is widely used in the purification of DNA and RNA.

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Synonym(s):
Proteinase K from Tritirachium album, Endopeptidase K
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.85

Quality Level

form

solid

mol wt

28.93 kDa

manufacturer/tradename

Novagen®

storage condition

OK to freeze

technique(s)

DNA extraction: suitable

shipped in

wet ice

storage temp.

2-8°C

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This Item
SAE0151SRE0005SRE0047
Millipore

Millipore

70663

Proteinase K, Lyophilized

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

manufacturer/tradename

Novagen®

manufacturer/tradename

-

manufacturer/tradename

-

manufacturer/tradename

-

storage condition

OK to freeze

storage condition

-

storage condition

-

storage condition

-

technique(s)

DNA extraction: suitable

technique(s)

-

technique(s)

-

technique(s)

-

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

General description

Proteinase K is a highly active 28,904-Daserine protease isolated from the fungusTritirachium album. The enzyme exhibitsbroad cleavage specificity on native anddenatured proteins and is widely used in thepurification of DNA and RNA. Its activityis increased in the presence of denaturantssuch as SDS (1%) and elevated temperature(50-60°C). The recommended workingconcentration is 50-100 µg/ml for proteinremoval and enzyme inactivation, and up to2 mg/ml for tissue treatment. The Proteinase K,Lyophilized powder can be prepared as a20 mg/ml stock solution in water and storedin aliquots at -20°C. The enzyme is alsoavailable as a ready-to-use concentrated stocksolution (600 mAU/ml) that is convenientfor routine use in most applications. 1 mgof Proteinase K is the equivalent of 30 mAU(AU = Anson unit). The Novagen ProteinaseK products are free of detectable DNase andRNase

Application

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 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.

Warning

Toxicity: Harmful (C)

Unit Definition

One AU (AU = Anson unit) is defined as the amount of enzyme that liberates 1.0 µmol (181 µg) of tyrosine from casein per minute at pH 7.5 at 37°C.

Legal Information

NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 1


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A Digaitiene et al.
Journal of applied microbiology, 112(4), 732-742 (2012-02-09)
To screen five strains of lactic acid bacteria (LAB) isolated from rye sourdoughs for the potential production of antimicrobial substances. Lactobacillus sakei KTU05-06, Pediococcus acidilactici KTU05-7, Pediococcus pentosaceus KTU05-8, KTU05-9 and KTU05-10 isolated from rye sourdoughs were investigated for the
Brooke G Pantazides et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 1121, 9-17 (2019-05-15)
Sulfur and nitrogen mustards are internationally banned vesicants listed as Schedule 1 chemical agents in the Chemical Weapons Convention. These compounds are highly reactive electrophiles that form stable adducts to a variety of available amino acid residues on proteins upon
Yang Sui et al.
Nucleic acids research, 50(12), 6890-6902 (2022-06-25)
Ribonucleotides can be incorporated into DNA during replication by the replicative DNA polymerases. These aberrant DNA subunits are efficiently recognized and removed by Ribonucleotide Excision Repair, which is initiated by the heterotrimeric enzyme RNase H2. While RNase H2 is essential
Cassandra Terry et al.
Open biology, 6(5) (2016-06-02)
Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel
Jae Wook Hyeon et al.
PloS one, 12(1), e0170266-e0170266 (2017-01-18)
Prion propagation is mediated by the structural alteration of normal prion protein (PrPC) to generate pathogenic prion protein (PrPSc). To date, compounds for the inhibition of prion propagation have mainly been screened using PrPSc-infected cells. Real time-quaking-induced conversion (RT-QuIC) is

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