Proteinase K (≈28.9 kDa) is a broad-spectrum, highly stable serine protease widely used in molecular biology to digest proteins and inactivate nucleases, ensuring high-quality DNA and RNA during extraction procedures. The enzyme is inhibited by classical serine protease inhibitors such as PMSF and DFP, and its activity diminishes upon exposure to temperatures above 95°C.
Proteinase K is typically supplied as a concentrated stock solution (e.g., ~20 mg/mL) in sterile water or in a stabilizing buffer such as 50 mM Tris (pH 8.0) with 1 mM CaCl₂, which supports long-term stability at 4°C. The enzyme shows optimal activity over a wide pH range (7.5–12.0), allowing compatibility with various extraction and lysis formulations.
In molecular workflows, Proteinase K is generally used at moderate working concentrations (up to ~50 μg/mL), providing efficient digestion of contaminating proteins and complete inactivation of endogenous nucleases. Its resilience to denaturing agents, broad pH tolerance, and strong proteolytic capacity make it an essential component of DNA/RNA purification and other protein-removal applications.
The Proteinase K developed in our laboratory is meticulously formulated to ensure exceptional performance in molecular biology and biotechnology applications. The Proteinase K undergoes stringent purification processes for removing impurities and contaminants that can ensure maximum enzymatic activity. It efficiently digests proteins, including native, denatured, and insoluble proteins, making it versatile for various experimental needs. It is also suitable for DNA and RNA extraction, protein digestion, tissue and cell lysis, decontamination, and PCR cleanup, our Proteinase K solution offers versatility across molecular biology workflows.



