Benzonase Nuclease, 90%
Escherichia Coli.
Greater than 90% as determined by SDS-PAGE.
Description
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds.
Benzonase Nuclease is purified by proprietary chromatographic techniques.
Product Specs
Benzonase Nuclease, derived from Serratia marcescens, is an enzyme known for its ability to degrade nucleic acids. Its high specific activity makes it effective in eliminating nucleic acid impurities from protein samples, a crucial step in various biotechnological and pharmaceutical applications. Benzonase Nuclease achieves this by breaking down DNA and RNA, reducing viscosity and improving the purity of the target protein. This enzymatic activity is also believed to play a role in the self-destruction of microorganisms.
This recombinant Benzonase Nuclease is produced in E. coli and is a single-chain polypeptide with 245 amino acids. The protein is non-glycosylated, has a molecular weight of 30kDa, and contains two disulfide bonds, which are essential for its activity. The enzyme is purified using advanced chromatographic methods to ensure high purity and activity.
This Benzonase Nuclease solution is formulated in a buffer containing 50% glycerol, 50 mM Tris-HCl (pH 8.0), 20 mM NaCl, and 2 mM MgCl2. This specific formulation helps to maintain the enzyme's stability and activity.
The purity of this Benzonase Nuclease is determined by SDS-PAGE analysis and is greater than 90%.
One unit (U) of Benzonase Nuclease is defined as the amount of enzyme needed to cause a change in absorbance at 260 nm (ΔA260) of 1.0 in 30 minutes. This corresponds to the complete digestion of 37 micrograms of DNA. The standard assay conditions are: 1 mg/ml of sonicated DNA substrate in a buffer containing 50 mM Tris-HCl (pH 8.0), 0.1 mg/ml BSA, and 1 mM MgCl2, incubated at 37°C.
Escherichia Coli.
Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product:
5’-mono-phosphate terminated oligonucleotides (3-5 bases).
Protease Activity: Not detectable
Product Science Overview
Benzonase Nuclease is a dimeric protein with a molecular weight of approximately 30 kDa . It contains two essential disulfide bonds that are crucial for its stability and activity . The enzyme functions by cleaving nucleic acids into 5′-monophosphate terminated oligonucleotides of 3 to 5 bases in length . This makes it an ideal tool for removing nucleic acids from protein samples, ensuring high purity and quality .
Benzonase Nuclease is widely used in various research and industrial applications, including:
- Protein Purification: It is used to remove nucleic acids from protein samples, enhancing the purity and quality of the final product .
- Cell Lysis: It is included in lysis buffers to digest DNA and RNA, facilitating the complete release of nuclear proteins .
- Immunoprecipitation: It is used to release protein complexes from the nucleoplasm and chromatin .
- Decellularization: It is employed in methods to remove residual nucleic acids from tissues, such as aortic roots .
The recombinant form of Benzonase Nuclease offers several advantages:
- High Specific Activity: It possesses exceptionally high specific activity, making it effective over a wide range of conditions .
- No Proteolytic Activity: It degrades nucleic acids without affecting proteins, ensuring the integrity of protein samples .
- Versatility: It can degrade all forms of DNA and RNA, making it suitable for various applications .
