Skip to Content
Merck
CN

E006556

Proteinase K from Tritirachium album

Synonym(s):

Endopeptidase K

Sign In to View Organizational & Contract Pricing.

Select a Size


About This Item

CAS Number:
UNSPSC Code:
12352204
EC Number:
254-457-8
MDL number:
EC Number:
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

mol wt

28.93 kDa

Looking for similar products? Visit Product Comparison Guide

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.

Regulatory Information

新产品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

If you need assistance, please contact Customer Support

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Ester Vázquez-Fernández et al.
PloS one, 7(11), e50111-e50111 (2012-11-28)
Elucidation of the structure of PrP(Sc) continues to be one major challenge in prion research. The mechanism of propagation of these infectious agents will not be understood until their structure is solved. Given that high resolution techniques such as NMR
Micaela Pivato et al.
PloS one, 7(12), e50027-e50027 (2012-12-29)
The aggregation of α-synuclein into amyloid fibrils constitutes a key step in the onset of Parkinson's disease. Amyloid fibrils of α-synuclein are the major component of Lewy bodies, histological hallmarks of the disease. Little is known about the mechanism of
Enzymatic sculpting of nanoscale and microscale surface topographies.
Jen-Huang Huang et al.
Angewandte Chemie (International ed. in English), 51(38), 9619-9623 (2012-08-29)
Xinping Lin et al.
Yeast (Chichester, England), 29(11), 467-474 (2012-10-16)
Red yeasts hold great promise in the production of microbial lipids and carotenoids. Genetic study of red yeasts has attracted much attention; however, rapid amplification of genes from red yeast samples remains technically challenging. Here a highly efficient method for
Sudhir Kumar Shukla et al.
The Journal of antibiotics, 66(2), 55-60 (2012-11-15)
The dominant role of biofilm-associated protein (Bap) in Staphylococcus aureus biofilm development prompted us to investigate Bap as a potential target for proteinase-mediated biofilm dispersion. Biofilm assay in microtitre plates showed that proteinase K hampered the early adhesion of cells

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

Contact Technical Service