Proteinase K from Tritirachium album, SERVA Electrophoresis

Proteinase  derived from Tritirachium album is a serine protease with very broad range of action: cleaves peptide bonds at the carboxylic side of aliphatic, aromatic, and hydrophobic amino acids. Suitable for the isolation of DNA and RNA.

• Mw 28.000
• Solution 20 mg/ml, min. 30 miliAnson-U/mg

Unit definition: 1 unit is defined as the amount of enzyme that liberates Folin-positive amino acids and peptides, corresponding to 1 µmol tyrosine per minute at 37 °C and pH 7.4 using urea-denatured hemoglobin as substrate.

Activities in other units: min. 8 DMC-U/mg. One DMC-Unit is that amount of enzymatic activity which catalyzes the cleavage of 1 µmole equivalent peptide bond from dimethylcasein per minute at 25 °C, pH 7.0, expressed in terms of the appearance of new terminal amino groups.

Inhibitors for Proteinase: AEBSF (cat. no. 12745), (PEFABLOC® SC (cat.no. 31682), PMSF (cat. no. 32395) and Diisopropylfluorophosphate (cat. no. 77205).

Extraneous activities: DNases and RNases not detectable.

Storage Temperature: -15 °C to -25 °C

HS: 38220000