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1.07393

Sigma-Aldrich

Proteinase K

(from Tritirachium album) solution in Tris/HCl pH 7.5; 0.01 mol/l; 600 mAnson-U/ml; for molecular biology EC 3.4.21.14

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Synonym(s):
ProK, native proteinase K solution, non-specific protease

Quality Level

form

liquid

pH

7.5 (25 °C in H2O, undiluted)

density

1.10 g/cm3 at 20 °C

storage temp.

2-8°C

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This Item
PRON-RO53947010791156001
Sigma-Aldrich

Sigma-Aldrich

1.07393

Proteinase K

Pronase from Streptomyces griseus

Roche

PRON-RO

Pronase

pH

7.5 (25 °C in H2O, undiluted)

pH

-

pH

-

pH

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

-

Quality Level

400

Quality Level

100

Quality Level

200

Quality Level

-

density

1.10 g/cm3 at 20 °C

density

-

density

-

density

-

General description

Proteinase K is an endopeptidase that belongs to the subtilisin family of proteinases. The polypeptide chain contains 278 amino acids with the catalytic triad Asp39, His69, Ser224.

Application

Proteinase K has been used:
  • to de-crosslink immunoprecipitated samples
  • to treat the poly-L-lysine coated slides of colon tissues for terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) assay
  • in in situ hybridization

Biochem/physiol Actions

Proteinase K catalyzes the hydrolysis of esters and peptide bonds. It is used with non-aqueous hydrated solvents for synthesizing peptides. Proteinase K is used to break the cross-linking that develops secondary to formalin fixation and expose the target sequence for primers and polymerase.

Analysis Note

Appearance (colour): colourless
Appearance (clearness): clear
Activity (hemoglobin; pH 7.5; 37 °C): ≥ 600 mAnsonU/ml
Spec. activity (calc. on protein): ≥ 40.0 mAnsonU/mg
DNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectable
RNases (RNA; 2 h; 37°C): not detectable
Colony count (aerobic bacteria): ≤ 10 CFU/ml

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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25G
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F Chavagnat et al.
Applied and environmental microbiology, 65(7), 3001-3007 (1999-07-02)
The general aminopeptidase PepN from Streptococcus thermophilus A was purified to protein homogeneity by hydroxyapatite, anion-exchange, and gel filtration chromatographies. The PepN enzyme was estimated to be a monomer of 95 kDa, with maximal activity on N-Lys-7-amino-4-methylcoumarin at pH 7
María Isabel Navarro-Mendoza et al.
Current biology : CB, 29(22), 3791-3802 (2019-11-05)
Centromeres are rapidly evolving across eukaryotes, despite performing a conserved function to ensure high-fidelity chromosome segregation. CENP-A chromatin is a hallmark of a functional centromere in most organisms. Due to its critical role in kinetochore architecture, the loss of CENP-A

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 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.

Guidelines on use of proteinase K, an enzyme commonly used to degrade proteins, and protect DNA and RNA from degradation in samples.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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