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P2308

Sigma-Aldrich

Proteinase K from Tritirachium album

lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology

Synonym(s):

Endopeptidase K

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

grade

for molecular biology

Quality Level

product line

BioUltra

form

lyophilized powder

specific activity

≥30 units/mg protein

mol wt

28.93 kDa

composition

Protein, ≥90% biuret

impurities

≤1 ppm DNA

foreign activity

DNAse, Nickase and RNAse, none detected

shipped in

wet ice

storage temp.

−20°C

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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.

Unit Definition

One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

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Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

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Mamoru Oshiki et al.
Frontiers in microbiology, 9, 830-830 (2018-05-15)
Detection and genotyping of pathogenic RNA viruses in human and environmental samples are useful for monitoring the circulation and prevalence of these pathogens, whereas a conventional PCR assay followed by Sanger sequencing is time-consuming and laborious. The present study aimed
Margarita Zayas et al.
PLoS pathogens, 12(1), e1005376-e1005376 (2016-01-05)
Hepatitis C virus (HCV) nonstructural protein (NS)5A is a RNA-binding protein composed of a N-terminal membrane anchor, a structured domain I (DI) and two intrinsically disordered domains (DII and DIII) interacting with viral and cellular proteins. While DI and DII
Mark F Sabbagh et al.
eLife, 7 (2018-09-07)
Vascular endothelial cell (EC) function depends on appropriate organ-specific molecular and cellular specializations. To explore genomic mechanisms that control this specialization, we have analyzed and compared the transcriptome, accessible chromatin, and DNA methylome landscapes from mouse brain, liver, lung, and
Bahram Peivastegan et al.
BMC plant biology, 19(1), 262-262 (2019-06-19)
Stored potato (Solanum tuberosum L.) tubers are sensitive to wet conditions that can cause rotting in long-term storage. To study the effect of water on the tuber surface during storage, microarray analysis, RNA-Seq profiling, qRT-PCR and phytohormone measurements were performed
Sreenivas Adurthi et al.
Scientific reports, 7(1), 17289-17289 (2017-12-13)
Oestrogen controls Foxp3 expression in regulatory T cells (Treg cells) via a mechanism thought to involve oestrogen receptor alpha (ERα), but the molecular basis and functional impact of ERα signalling in Treg cells remain unclear. We report that ERα ligand

Articles

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

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

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

Pro K aids in disrupting cell membranes for DNA release, crucial for downstream molecular biology techniques.

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