LeaBiozyme® Benzonase

• Synonyms:

  Benzonase

• Expression System:

  E.coli

• Tag:

  Tag free

• Applications:

  1. Removal of DNA contamination from vaccine and virus sample preparation. 2. Nucleic acid contamination was removed during protein extraction: During recombinant protein purification or protein extraction from tissue cell samples, Benzonase can effectively reduce the sample viscosity, Benefits downstream operations. 3. Used in combination with cell or bacterial lysates to remove nucleic acids from crude extracts, reducing solution viscosity and enhancing protein yield. 4. Prevention of clot formation in peripheral blood mononuclear cells (PBMCs) with limited storage. 5. Degrading nucleic acids, Conducive to the preparation of high-quality inclusion bodies before renaturation of insoluble proteins. 6. Effectively remove the influence of negatively charged nucleic acids on two-way SDS-PAGE protein samples, improve the separation effect of protein and enhance the resolution of 2-DE.

• Endotoxin:

  < 1.0 EU per μg of the protein as determined by the LAL method.

• Purity:

  ≥ 99% as determined by SDS-PAGE and HPLC analysis.

• Activity:

  Enzyme activity units are defined by measuring the ability to hydrolyze herring sperm DNA substrate (Herring Sperm DNA, Sigma, catalog number 07290) . One unit of Benzonase activity is defined as the amount of enzyme that causes a decrease in A260nm of 1.0 within 30 minutes under reaction conditions of 37°C and pH 8.0 (equivalent to complete digestion of 37 ug of DNA), with a specific activity greater than 1.0 x 10^6 U/mg.

• Length:

  246

• Form:

  Liquid

• Buffer:

  20 mM Tris-HCl (pH 8.0), 20 mM NaCl, 2 mM MgCl2, and 50% glycerol

• Molecular Weight:

  26.8 kDa

• Storage Conditions:

  Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles. If the package is opened and stored at 4°C for more than one week, it is recommended to sterilize the product using a filter to prevent microbial contamination.

• Symbol:

  Benzonase

• Species:

  Serratia marcescens

• Overview:

  Benzonase (EC 3.1.30.2) is a non-specific endonuclease derived from Serratia marcescens, known as Serratia marcescens endonuclease. The enzyme was expressed and purified from Escherichia coli strain W3110. This strain is a mutant of the K12 strain, the pET41 production plasmid was contained. In terms of structure, the protease is homodimer, the molecular weight of the single subunit is 26.8kDa, it is composed of 246 amino acids, Two pairs of disulfide bonds essential for activity, Mg2＋ is its activator. The enzyme can degrade any form of DNA and RNA (linear, circular, supercoiled) into oligonucleotides of 3-5 base pairs, while maintaining high efficiency under a wide range of operating conditions. We can provide a highly pure (>99% by SEC-HPLC) universal nucleic acid enzyme with specific activity of up to 2 x 10^6 U/mg, endotoxin levels below 1 EU/mg, and free from detectable protease activity and viral contaminants. We have directional protein refolding technology (LeaBioFOLD) and self-developed technology platforms for proteins covering screening and purification, engineering design, fixed-point coupling design, and dosage form development. Protein refolding is a process of recovering protein aggregates in inclusion bodies in the form of misfolded and inactive proteins expressed by prokaryotes such as Escherichia coli back into proteins with correct conformation and bioactivity under appropriate conditions in vitro. It is a key technology for biopharmaceutical companies but a major bottleneck in protein production in prokaryotic expression systems. Leading Biology has been specializing in protein refolding for many years, has a core team with over ten years of experience in this technology and rich experience in its industrialization. Our team is summarizing the experience to form an independent technological system of ours.