DNase / RNase Free High Purity Recombinant Proteinase K 39450-01-6

Proteinase K, a broad-spectrum serine protease under the subtilisin-like class, belongs to Peptidase family S8. The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. This makes it a broad spectrum proteinase. Proteinase K is activated by calcium (1 – 5 mM), it digests proteins preferentially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Although calcium ions do not affect the enzyme activity, they do contribute to its stability. Proteins will be completely

digested, if the incubation time is long and the protease concentration high enough.

Healthegn Biotech express and purify the recombinant proteinase K (rProK) from yeast (Pichia Pastoris) based on the optimized gene of Engyodontium album by site-directed mutation. The rProK possesses a high specific activity which remains stable over a wide range of temperatures and pH values with substantially increased activity at higher temperature. Purified by chromatography process, the rProK has a high purity more than 95%, which is also completely free of DNase and RNase activities. The rProK can be used in a variety of molecular biology, cell biology and other related experiments, such as genomic DNA extraction, enzyme digestion and removal, cell permeability and so on.

Source: Yeast

Molecular weight: 29kD

Purity: More than 95%

Bioactivity: ≥30U/mg detected using hemoglobin as substrate

E.C. No.: 3.4.21.64

DNase:Non-detection

RNase: Non-detection

Storage Conditions: store at 4 °C

Shelf Life: 24 months