Nucleic Acid Extraction Recombinant Proteinase K 29kD ProK 39450-01-6

Proteinase K, a broad-spectrum serine protease, firstly was extracted and purified from Engyodontium album. Because it can degrade Keratin, so named proteinase K. The crystallization and molecular structure of Proteinase K indicate it belongs to subtilisin family, whose active site has a characteristic catalytic triple amino acid Asp39-His69-Ser224. Proteinase K has no significant substrate specificity, and main cleavage site is the peptide bond at the carboxyl end of the hydrophobic amino acid such as aliphatic or aromatic.

Recombinant Proteinase K (rProK) is derived from yeast based on the optimized gene of Engyodontium album by site-directed mutation. It is purified by chromatography process, and with calcium and glycerin as protective agents. The rProK can be widely used in the purification of nucleic acid from tissues or cell lines. Because it is tested for the absence of RNases and DNases, it is also ideal for isolating PCR and RT-PCR templates. The activity of Proteinase K is elevated temperature (50-60°C). The recommended working concentration is 50-100 μg/mL for protein removal and enzyme inactivation and up to 2 mg/mL for tissue treatment.

• Source: Yeast (Pichia Pastoris)
• Molecular weight: 29kD
• Bioactivity: ≥30U/mg detected using hemoglobin as substrate
• E.C. No. 3.4.21.64
• DNase Non-detection
• RNase Non-detection

The advantages of recombinant proteinase K from Healthgen Biotech:

• High activity - broad-spectrum serine protease
• Active under denaturing conditions - useful for a variety of applications
• Stable - at high temperatures
• Molecular biology grade - useful for general digestion of proteins
• Two formats - lyophilized powder and liquid