Proteinase K is an enzyme commonly used in molecular biology for various applications due to its ability to digest proteins. Its primary function is to cleave peptide bonds within proteins, resulting in their degradation. This enzyme is particularly known for its robustness and effectiveness in breaking down a wide range of proteins, including those that are normally resistant to other proteases.

Here are some of the key functions and applications of Proteinase K:

DNA and RNA Extraction: Proteinase K is often used in nucleic acid extraction protocols to remove proteins that might interfere with downstream applications such as PCR (Polymerase Chain Reaction) or sequencing. It helps in releasing DNA and RNA from cells or tissues by breaking down the associated proteins.

Tissue Lysis: Proteinase K is utilized in tissue lysis protocols to disrupt cell membranes and break down structural proteins, allowing access to intracellular components.

Gene Cloning and Manipulation: In molecular biology, Proteinase K treatment is employed in various gene cloning and manipulation techniques to remove unwanted proteins or to inactivate enzymes that might interfere with the experimental process.

Protein Structure Studies: Proteinase K is also used in protein structure studies to selectively digest specific proteins from a complex mixture, enabling the isolation and characterization of individual proteins.

In situ Hybridization: In molecular biology techniques such as in situ hybridization, where the localization of specific nucleic acid sequences within tissues is studied, Proteinase K treatment is often used to remove proteins and improve the accessibility of the target sequences to nucleic acid probes.

Removal of RNase: Proteinase K treatment is sometimes employed to remove RNase (ribonuclease) contamination from experimental samples, as Proteinase K digestion can render RNases inactive.

Overall, Proteinase K is a versatile enzyme with broad applicability in molecular biology, genetics, biochemistry, and other related fields, owing to its ability to efficiently digest proteins under various experimental conditions.

At SBS Genetech, we proudly present a groundbreaking solution to this demand with its Mutant Proteinase K. Engineered through cutting-edge technology, this enzyme stands as a superior alternative to the wild-type Proteinase K, offering heightened performance and versatility across a myriad of applications.

Enhanced Properties

The hallmark feature of Mutant Proteinase K lies in its superior specific activity and enhanced stability, even at room temperature, setting it apart from its conventional counterpart. This non-specific serine proteinase boasts a broad substrate spectrum, ensuring efficacy in digesting both native and denatured proteins across diverse experimental setups.

Robust Characteristics

Mutant Proteinase K exhibits remarkable resilience, maintaining its activity over a wide pH range from 4 to 12. This adaptability renders it suitable for a multitude of experimental conditions, accommodating various research requirements with ease. Its compatibility with different substrates and experimental setups makes it an indispensable tool for molecular biologists and researchers alike.

Product Specifications

Designed to meet the exacting standards of the scientific community, Mutant Proteinase K is available in meticulously crafted formulations:

• Cat. No.: MPTK-10 (for 10g), MPTK-1000 (for 1kg)
• Form: White Powder, Lyophilized from purified solids or liquid enzyme
• Specific Activity: ≥30 U/mg dry weights
• Package: 100 mg/bottle (Standard) or customizable packing options ranging from 1 to 200 grams
• Source: Pichia Pastoris with a mutant cloned gene from Tritirachium album limber
• Molecular Weight: 29,300

Preparation and Storage

Mutant Proteinase K is conveniently soluble in water, yielding a clear, colorless solution at a concentration of 1 mg/ml. For optimal storage and longevity, it is recommended to store the enzyme below 4°C. With a shelf life of three years for powder and one year for liquid formulations, researchers can trust in its reliability for long-term experiments.

Quality Assurance

Stringent quality control assays validate the potency and purity of Mutant Proteinase K:

• Unit Definition: Defined as the amount of enzyme liberating 1 µmol of tyrosine per minute from casein at 37°C, pH 7.5.
• DNase and RNase Activity: Undetectable after prolonged incubation with DNA and RNA, respectively.
• Protein Purity: Exceeds 99% as confirmed by Native-PAGE and SDS-PAGE assays.

Versatile Applications

The versatility of Mutant Proteinase K is showcased through its wide-ranging applications, mirroring those of wild-type Proteinase K but with enhanced performance. From isolating mRNA and genomic DNA to modifying glycoproteins for structural studies, this enzyme proves indispensable in various molecular biology endeavors. Active in the presence of SDS, urea, and EDTA, and functional within a broad temperature range of 15°C to 75°C, its adaptability knows no bounds.

Scientific Validation

Backed by extensive research, Mutant Proteinase K has garnered recognition in esteemed scientific journals, including its inclusion in the New Products section of the Science Journal on March 8, 2019. This recognition underscores its significance and contribution to advancing molecular biology research.

Conclusion

SBS Genetech's Mutant Proteinase K stands as a testament to innovation and excellence in the field of molecular biology. With its unparalleled performance, enhanced stability, and broad applicability, it emerges as an indispensable tool for researchers worldwide. As a leading industry player in the Proteinase K market, SBS Genetech continues to spearhead advancements, empowering scientists in their quest for knowledge and discovery.

Related: 

• Mutant Proteinase K: for common molecular biology applications
• Mutant Proteinase K (Sterile): for high-standard applications
• Mutant Proteinase K (Industrial Grade): for industrial applications