E006556
Proteinase K from Tritirachium album
Synonym(s):
Endopeptidase K
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CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
mol wt
28.93 kDa
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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.
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.
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Karine Berthelot et al.
PloS one, 7(10), e48065-e48065 (2012-11-08)
REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be
Maria Angela de Mello Marques et al.
Journal of microbiological methods, 91(3), 487-489 (2012-10-02)
Six commercially available DNA extraction kits, as well as thermal lysis and proteinase K DNA extraction were evaluated regarding bacterial inactivation, DNA yield and purity, and their use in a Burkholderia pseudomallei real-time PCR. While all methods successfully inactivated the
Wu-Ling Xie et al.
International journal of molecular medicine, 31(1), 81-90 (2012-11-24)
Fatal familial insomnia (FFI) is an autosomal dominant prion disease clinically characterized by rapidly progressive insomnia, prominent autonomic alterations and behavioral disturbance. The D178N mutation of the prion protein gene (PRNP) on chromosome 20 in conjunction with methionine at codon 129
Protein-protected Au clusters as a new class of nanoscale biosensor for label-free fluorescence detection of proteases.
Yucai Wang et al.
Small (Weinheim an der Bergstrasse, Germany), 8(24), 3769-3773 (2012-09-13)
Natallia Makarava et al.
The Journal of biological chemistry, 288(1), 33-41 (2012-11-22)
With the development of protein misfolding cyclic amplification (PMCA), the topic of faithful propagation of prion strain-specific structures has been constantly debated. Here we show that by subjecting brain material of a synthetic strain consisting of a mixture of self-replicating
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