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MilliporeSigma

70663

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.

Synonym(s):

Proteinase K from Tritirachium album, Endopeptidase K

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100 MG

$171.00

500 MG

$558.00

$171.00


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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.85

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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
SRE0047SAE01511.24568
technique(s)

DNA extraction: suitable

technique(s)

-

technique(s)

-

technique(s)

-

form

solid

form

lyophilized powder

form

-

form

solid

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

-

storage condition

OK to freeze

storage condition

-

storage condition

-

storage condition

-

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

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.
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.

Other Notes

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

Disclaimer

Toxicity: Harmful (C)

pictograms

Health hazardExclamation mark

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


Certificates of Analysis (COA)

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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
Jai Rautela et al.
Cancer immunology research, 3(11), 1207-1217 (2015-07-23)
Metastatic progression is the major cause of breast cancer-related mortality. By examining multiple syngeneic preclinical breast cancer models in mice lacking a functional type-I interferon receptor (Ifnar1(-/-) mice), we show that host-derived type-I interferon (IFN) signaling is a critical determinant
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
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
Lydia Kapsenberg et al.
iScience, 25(8), 104677-104677 (2022-07-19)
Predicting the potential for species adaption to climate change is challenged by the need to identify the physiological mechanisms that underpin species vulnerability. Here, we investigated the sensitivity to ocean acidification in marine mussels during early development, and specifically the

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