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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

Synonyme(s) :

ProK, native proteinase K solution, non-specific protease

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About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.51

Niveau de qualité

400

Forme

liquid

pH

7.5 (25 °C in H2O, undiluted)

Densité

1.10 g/cm3 at 20 °C

Température de stockage

2-8°C

Description générale

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

Actions biochimiques/physiologiques

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.

Remarque sur l'analyse

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

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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.

Proteinase K: Introduction & Applications

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

Proteinase K: Introduction & Applications

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

Proteinase K: Introduction & Applications

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

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