High quality Enzyme Proteinase K 39450-01-6 with stock

Proteinase K，Recombinant Proteinase K

Form: Lyophilized White Powder.
Source: Mutated gene from Tritirachium limber, Expressed in recombinant yeast.
Specific Activity: ≥34U/mg dry weights
Package: 100mg/Bottle, 1g/Bottle (Standard) or 1-200 gram Customer packing.
Storage Conditions:Store at 4 to -20ºC recommended.
Mutated Proteinase K powder is stable at room temperature in 3 years.
Expiration : Three years if kept below 4ºC.
Molecular Weight: 29,300 D
QC Assays:
Activity Assay and Unit Definitions:
 One unit is defined as the amount of enzyme that will liberate 1 μmol of tyrosine per minute at 37º C, pH7.5.
DNase Activity: none detectable enzyme activity with λ DNA after 6 hours incubation at 37ºC.
RNase Activity: none detectable of ribnuclease activity after 16 hours incubation at 25 º C
Protein Purity: over 99% (Native-PAGE and SDS-PAGE assay)

Applications:
The application of this Mutated Proteinase K is similar with wild type Proteinase K. But the mutated one has higher specific activity and more stable at RT. It is a broad substrate non-specific serine Proteinase. It is active over the pH range 4-11. It was used on any situation to digest native and denatured proteins. For instance, it is used for isolating mRNA or genomic DNA from different tissues and modifying glycoprotein for structure studies.Mutated Proteinase K is active with SDS, urea and EDTA and active between the temperature15-75ºC.

Now,Proteinase K is a broad substrate non-specific serine proteinase. It was used on isolating mRNA, genomic DNA and digesting unwanted proteins during DNA and RNA preparations from different kinds of cells.

It’s been used on glycoprotein modification and protein structure studies also. Proteinase K is active with SDS, urea and EDTA.
Proteinase K is used for the isolation of native high molecular genomic nucleic acids. Enzymes like DNases and RNases from microorganisms and mammalian cells are rapidly inactivated by Proteinase K.
Adding Proteinase K already during the cell lysis enables the isolation of highly native undamaged high molecular DNA or RNA. A variety of methods have been established, which are documented in numerous publications.
Recently, Proteinase K has been used for the detection of BSE forming proteins which are uniquely resistant towards the enzyme's proteolytic cleavage.
Proteinase K is very useful in the analysis of membrane structure by means of modification of proteins and glycoproteins on cell surfaces.
Because of the cleavage specificity Proteinase K, characteristic fragments of proteins are obtained which are helpful in revealing the structure and function of proteins, particularly enzymes.