Proteinase K Solution (20 mg/mL, mNGS-Grade, RNase-Free, DNase-Free)
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Proteinase K Solution (20 mg/mL, mNGS-Grade, RNase-Free, DNase-Free)

Cat.No: IVDRM-0187 Datasheet

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Product Name Proteinase K Solution (20 mg/mL, mNGS-Grade, RNase-Free, DNase-Free)
Catalog No. IVDRM-0187
Description Proteinase K is a broad-spectrum serine protease with a molecular weight of approximately 29.3 kDa that cleaves peptide bonds at the carboxyl side of aliphatic and aromatic amino acids. It is widely used for preparing chromosomal DNA for pulsed-field gel electrophoresis, Western blotting, and removing nucleases from DNA and RNA preparations. Denaturants such as 1% SDS enhance its activity, and the commonly used working concentration is 50-100 µg/mL, adjusted according to buffer composition (SDS, urea), pH, and temperature. This ready-to-use solution is a low-residue formulation: while preserving the intrinsic properties of the enzyme, it carries a significantly lower microbial background, ensuring greater accuracy in downstream detection such as metagenomic next-generation sequencing (mNGS).
Intended Use Protein digestion during nucleic acid extraction and purification; metagenomic next-generation sequencing (mNGS) workflows requiring low microbial background.
Principle / Technology A serine protease that cleaves peptide bonds carboxyl-terminal to aliphatic and aromatic amino acids, degrading proteins and inactivating nucleases in nucleic acid samples.
Sample Type DNA and RNA preparations; samples for mNGS and other downstream molecular detection assays.
Performance Range / Specifications Specific activity: ≥800 U/mL.
Protein concentration: ≥20 mg/mL.
Active in the presence of urea and SDS.
Active over a broad pH range of 4.5-12.5, with an optimal pH range of 7.0-12.0.
Typical working concentration: 50-100 µg/mL.
Specificity Cleaves peptide bonds at the carboxyl side of aliphatic and aromatic amino acids. Certified free of RNase and DNase activity.
Reaction Conditions / Protocol Incubate in reaction buffer at 37-65°C for 1 hour; a reaction temperature of 65°C is recommended. The working concentration (commonly 50-100 µg/mL) should be optimized according to the presence of SDS or urea, pH, and temperature.
Components / Formulation Ready-to-use Proteinase K solution at 20 mg/mL, RNase-free and DNase-free.
Storage Conditions Store at 2-8°C. For longer-term storage, keep frozen at -25 to -15°C.
Shelf Life 2 years when stored at 2-8°C.
Package Specifications 1 mL; 5 mL; 100 mL; 1000 mL
Product Form Solution (20 mg/mL)
Quality Control Free of RNase and DNase. Low-residue formulation with reduced background microbial carryover to safeguard the accuracy of downstream mNGS detection. Specific activity ≥800 U/mL; protein concentration ≥20 mg/mL.
Concentration ≥20 mg/mL
Activity / Unit Definition One unit is defined as the amount of enzyme that hydrolyzes casein to release 1 µmol of L-tyrosine per minute under the specified conditions. Specific activity: ≥800 U/mL.
Molecular Weight Approximately 29.3 kDa
Source / Origin Tritirachium album
pH Range / Optimal pH Active from pH 4.5 to 12.5; optimal pH 7.0-12.0.
Expiration Date / Stability Stable for 2 years at 2-8°C; for extended storage, keep at -25 to -15°C.
Compatibility Activity is stable in the presence of urea and SDS; denaturants such as 1% SDS enhance activity.
Heat Inactivation Inactivate by adding PMSF or DFIP inhibitors to the reaction system.

For research use only, not for clinical use.

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