1.24568
Proteinase K
(from Tritirachium album) chromatographically purified lyophilized 30 mAnson-U/mg for biochemistry and molecular biology EC 3.4.21.14
Synonym(s):
Proteinase K from Tritirachium album, Tritirachium alkaline proteinase, Endopeptidase K
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Index Number:
254-457-8
NACRES:
NA.51
MDL number:
form
solid
mol wt
28.93 kDa
pH
6.2-6.8 (20 °C, 10 g/L in H2O)
density
1.1 g/cm3
bulk density
35 kg/m3
storage temp.
2-8°C
Quality Level
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Analysis Note
Appearance (color): white
Appearance (description): lyophilisate
Activity (hemoglobin; pH 7.5; 37 °C): ≥ 30.0 mAnsonU/mg
Spec. activity (calc. on protein): ≥ 40 mAnsonU/mg
DNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectable
RNases (RNA; 2 h; 37°C): not detectable
Appearance (description): lyophilisate
Activity (hemoglobin; pH 7.5; 37 °C): ≥ 30.0 mAnsonU/mg
Spec. activity (calc. on protein): ≥ 40 mAnsonU/mg
DNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectable
RNases (RNA; 2 h; 37°C): not detectable
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.
signalword
Danger
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein.
Jan P M Langeveld et al.
Veterinary research, 52(1), 59-59 (2021-04-18)
The unconventional infectious agents of transmissible spongiform encephalopathies (TSEs) are prions. Their infectivity co-appears with PrPSc, aberrant depositions of the host's cellular prion protein (PrPC). Successive heat treatment in the presence of detergent and proteolysis by a keratinase from Bacillus
L Bruno et al.
Immunity, 5(4), 343-352 (1996-10-01)
In peripheral lymphoid tissues of TCR transgenic mice that express the nominal antigen (HY peptide plus H-2Db MHC) recognized by the transgenic TCR, there exist unusual CD4-CD8- and CD4-CD8low cells bearing the transgenic TCR. Here we show that, unlike TCR
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The functional and structural characterization of macromolecular complexes requires protocols for their native isolation. Here, we describe a protocol for this task based on the recombinant poxvirus Vaccinia expressing tagged proteins of interest in infected cells. Tagged proteins and their
D L Baggesen et al.
Journal of clinical microbiology, 35(1), 330-333 (1997-01-01)
Studies of pairs of Salmonella enterica serovar Enteritidis isolates from different poultry flocks showed that phage type (PT) 7 may be derived from PT 1, 4, and 6. The conversion appeared to be associated with loss of lipopolysaccharide. It is
Takaharu Sasaki et al.
Cell reports, 28(1), 202-217 (2019-07-04)
Complex interactions between immune cells are an important component in the induction of obesity. Here, we show that Il2rg-/-Rag2-/- mice lacking all lymphocytes are resistant to diet-induced obesity. Transplantation of bone marrow cells from Rag2-/- mice, which lack only acquired
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Global Trade Item Number
| SKU | GTIN |
|---|---|
| 1.24568.0010 | 04022536217390 |
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