PROK Tritirachium album
Greater than 95% as determined by SDS-PAGE.
Description
Product Specs
We offer bulk quantities of recombinant Proteinase K.
For orders of 1,000 grams, the price is $100 per gram.
While recombinant Proteinase K is stable at room temperature, storage between 2°C and 8°C is recommended. Avoid freezing the product.
The purity of this product is greater than 95% as assessed by SDS-PAGE analysis.
The biological activity of this product is 36 Units/mg.
One unit is defined as the quantity of enzyme required to hydrolyze urea-denatured hemoglobin, resulting in a color equivalent to 1.0 µmol of tyrosine per minute at 37°C and pH 7.5. The colorimetric determination is performed using the Folin-Ciocalteu reagent.
Product Science Overview
Proteinase K is a highly active serine protease that was originally isolated from the fungus Tritirachium album. This enzyme is widely used in molecular biology for its ability to digest proteins and remove nucleases from DNA and RNA preparations. The recombinant form of Proteinase K is produced using various expression systems, such as Pichia pastoris, to ensure high purity and activity.
Proteinase K was first isolated from the fungus Tritirachium album. This fungus is known for its ability to grow on keratin, a tough protein found in hair, nails, and feathers. The enzyme was named “Proteinase K” due to its keratinolytic activity, meaning it can digest keratin. The enzyme belongs to the subtilisin family of proteases, which are characterized by their broad substrate specificity and stability under various conditions .
Proteinase K is a serine protease, which means it has a serine residue in its active site that plays a crucial role in its catalytic mechanism. The enzyme has a molecular weight of approximately 28.93 kDa and consists of a single polypeptide chain. The active site of Proteinase K contains a catalytic triad composed of aspartate, histidine, and serine residues. This triad is responsible for the hydrolysis of peptide bonds in proteins .
The recombinant form of Proteinase K is produced using various expression systems, such as Pichia pastoris. This yeast expression system is preferred due to its ability to produce high yields of active enzyme. The recombinant enzyme is identical to the native enzyme in terms of amino acid sequence and molecular structure. The production process involves the insertion of the gene encoding Proteinase K into the yeast genome, followed by fermentation and purification to obtain the active enzyme .
Proteinase K is widely used in molecular biology and biotechnology due to its broad substrate specificity and stability under various conditions. Some of the key applications include:
- DNA and RNA Purification: Proteinase K is used to digest proteins and remove nucleases from DNA and RNA preparations, ensuring high-quality nucleic acids for downstream applications.
- Protein Digestion: The enzyme is used to digest proteins in various biological samples, including tissues, cells, and microorganisms.
- Prion Research: Proteinase K is used to enrich prion proteins from brain tissue samples for research on transmissible spongiform encephalopathies (TSEs).
- Antigen Retrieval: The enzyme is used to treat paraffin-embedded tissue sections to expose antigen binding sites for antibody labeling .
