Proteinase K CAS 39450-01-6
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- Appearance: White powder
- Assay: 99. 0%min
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Proteinase K: The Complete Guide
Proteinase K for Sale
Basic Info of Proteinase K
What is Proteinase K?
Proteinase K is a powerful proteolytic enzyme separated from Yeast infection albicans. It has high specific activity as well as is a vital reagent for DNA removal. The enzyme is active in a vast array of pH (4-12.5) as well as high temperature (50-70 ° C), and also is used for the splitting up of plasmid or genomic DNA and also RNA.
Proteinase K can digest all-natural keratin, so it is named proteinase K. The primary cleavage websites are the carboxyl incurable peptide bonds of aliphatic as well as aromatic amino acids. It is commonly used in the laboratory due to its comprehensive reducing capacity. This protease belongs to the S8 family of serine protease sb superfamily (subtilisin also belongs to this superfamily). The molecular weight of proteinase K was 28.9 kilodaltons.
Proteinase K is a serine protease related to subtilisin, which is stemmed from Candida albicans Linnaeus. It is named proteinase K since it can degrade keratin. It is an extremely energetic broad-spectrum protease, which can still keep high enzyme task in denaturant urea or sodium dodecyl sulfonate (SDS) remedy, so it is commonly made use of in the extraction of DNA or RNA from numerous organic materials.
Proteinase K Uses
- Proteinase K can be used for proteolytic inactivation of nucleases in the process of DNA and also RNA splitting up.
- Endotoxin bound to cationic healthy proteins such as lysozyme and ribonuclease A is eliminated.
- Proteinase K has actually been reported that it can be made use of to separate mitochondria of liver, yeast and mung bean.
- Determine the location of the enzyme on the membrane.
- Paraffin embedded tissue sections were processed to expose antigen binding sites for antibody labeling.
- Prion proteins were digested from brain tissue samples in the infectious spongiform encephalopathy (TSE) study.
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Application of Proteinase K
Proteinase K is named proteinase K because of its ability to digest keratin (kratin). The proteinase K family contains a variety of intracellular peptidases secreted by fungi, yeast and Gram-negative bacteria, among which the enzymes secreted by bacteria have a high degree of sequence similarity (>55%). Candida albicans (Tritirachium albumLimber) secreted to produce proteinase K is the model protein of this family. Proteinase K has cleavage activity on most substrates, but prefers peptide chains with aliphatic and aromatic hydrocarbons. It is a serine protease with a typical serine active site: Asp39–His69–Ser224. It contains a single peptide chain with 277 amino acids, 2 disulfide bonds, a vacant cysteine site and two calcium ion binding sites.
The application of proteinase K is mainly to remove DNase and RNase during nucleic acid extraction, to remove histone bound to the genome, and to inactivate alkaline phosphatase. At present, molecular biology technology has been applied to many detection standards, such as genetically modified detection, animal attribute detection, pathogenic microorganism detection, etc. In molecular biology detection, the extraction quality of nucleic acid directly affects the amplification efficiency of subsequent PCR reactions. Many standards include the addition of proteinase K digestion to the nucleic acid extraction step in order to extract purer nucleic acids. In order to protect nucleic acids, molecular biology nucleic acid extraction experiments usually contain reagents such as EDTA. Since EDTA can complex with metal ions, the enzymatic activity may be affected; and digestion is usually carried out at pH 8.0 and 55 °C. Enzyme activity is affected by different pH and temperature conditions.