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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

Synonym(s):

ProK, native proteinase K solution, non-specific protease

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.51

Quality Level

400

form

liquid

pH

7.5 (25 °C in H2O, undiluted)

density

1.10 g/cm3 at 20 °C

storage temp.

2-8°C

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
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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: Introduction & Applications

Proteinase K aids in molecular biology applications by digesting structural proteins, removing nucleases, and isolating intact genomic DNA.

How Proteinase K Can Be Used in Blood DNA Extraction Applications

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.

Guide on How to Use Proteinase K in Different Procedures

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

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