Recombinant Proteinase K CAS:39450-01-6

1. Product introduction

Proteinase K is a non-specific endoproteinase, which is a serine protease that can cleave ester bonds and peptide bonds connected to the carboxyl ends of aliphatic amino acids, hydrophobic amino acids and aromatic amino acids. The molecular weight is *8.9 kDa (monomer). It is active at pH 4 to pH *2. It is also stable in the presence of SDS, urea or EDTA. It can cleave the carboxy terminal peptide bonds of aliphatic and aromatic amino acids, and is used for the degradation of proteins in biological samples. This enzyme has been decolorized and purified by chromatography to remove RNA and DNA, and the activity of other miscellaneous enzymes can not be detected. Because proteinase K is stable in urea and SDS, and has the ability to degrade natural proteins, the smallest polypeptide that is hydrolyzed is a tetrapeptide molecule.

2. Product advantages

High purity: no other miscellaneous enzyme activity: no other side reactions in the digestion reaction, high yield

High specific activity: specific activity not less than *0 u/mg protein

Electrophoresis purity: identified by SDS-PAGE electrophoresis, over *9%

Stable: freeze-dried powder, easy to store and transport

3. Product use

Mainly used in genetic diagnosis kits, genomic DNA extraction kits, RNA extraction kits to remove nucleases in DNA and RNA preparation, and can also be used to extract non-protein components from tissues to degrade protein-containing impurities, such as DNA vaccines and heparin Preparation, etc., can also prepare chromosomal DNA for pulse electrophoresis and Western blotting.

4. Product features

Source: Tritirachium album limber