PROTEINASE K Molecular Biology Grade from Parengyodontium album (Tritirachium album) is a subtilisin-related serine protease

This recombinant enzyme is expressed in Pichia pastoris, and undergoes extensive purification to yield the highest quality product.

Features

• Recombinant broad-spectrum non-specific protease derived from Tritirachium album and over-expressed in Pichia pastoris.
• High activity and exceptional purity (Molecular Biology Grade & NGS Grade).
• Active at high temperatures (up to 56°C) and denaturing conditions (e.g. in the presence of urea and/or SDS), what makes it ideal for digesting proteins in variety of applications.
• Stable over a wide pH range: 4.0–12.5 (optimum pH 7.5–8.0).
• Decreased amount of host DNA (≤ 10 pg/mg / MBG or ≤ 0.1 pg/mg NGS).
• Available as powder, lyophilized “cake” or liquid.

Applications:

• Extraction of DNA and RNA from different starting materials.
• Purification of target material from contaminating proteins.
• Removal of DNases and RNases during nucleic acids isolation.

Units

One unit of Proteinase K hydrolyzes urea-denaturated hemoglobin producing color equivalent of 1 μmol tyrosine per 1 min at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.