Recombinant Proteinase K (EC 3.4.21.64) from Tritirachium album is a highly stable serine protease with broad substrate specificity. It effectively degrades a wide range of native proteins, even in the presence of detergents. Evidence from crystal and molecular structure studies indicates this enzyme belongs to the subtilisin family with an active site catalytic triad (Asp39-His69-Ser224). 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. Its versatility makes it a widely used enzyme in molecular biology for protein digestion and nucleic acid purification.

Appearance: Colorless to light brown liquid
Activity: ≥800 U/ml
Protein concentration: ≥20 mg/ml
DNase, RNase, Nickase: None detected
Molecular weight: 29 kDa (SDS-PAGE)
Isoelectric point: 7.81

Optimum pH: 7.0-12.0
Optimum temperature: 65℃
pH stability: pH 4.5-12.5 (25℃, 16 hrs)
Thermal stability: Below 50℃ (pH 8.0, 30 min)
Storage stability: Over 90% activity for 12 months at 25℃
Activators: SDS, urea
Inhibitors: DFP, PMSF

One unit (U) is defined as the amount of enzyme required to hydrolyze casein to produce 1 μmol tyrosine per minute at 37℃.

Over 90% activity stored at 25℃ for 12 months. Recommended storage at 2-8℃.