BeaverBeads™ Magrose Protein G Antibody Purification

BeaverBeads™ Protein A, Protein G are superparamagnetic beads covalently coated with recombinant Protein A or Protein G that contains Fc binding domains for the purification of monoclonal or polyclonal antibodies from cell lysate, blood plasma, ascites and tissue culture supernatant, and for antibody immobilization studies. The one-step solution can reduce the antibody absorption process to 10 minutes and purification process to 30 minutes, yielding antibody with >90% purity.

• Packaging: 10% (v/v), 30-150 μm

1. Highly effective antibody binding capacity and ultra-low non-specific adsorption performance

• Protein A Matrix beads extract the purity of antibody IgG from 10-fold diluted human serum, which is substantially the same or even higher than the purity of IgG extracted directly from serum.

2. Time-saving, simple and mild

• No centrifugation, or magnetic separation can be used, and the use of the chromatograph-agarose gel purification system can greatly shorten the operating time
• Avoid the error of the packing loss caused by repeated suction fluid
• Avoid damage to active protein by mechanical shearing force in centrifugation

3. High product stability

• BeaverBeads ™ Protein A Matrix Magnetic Beads Stability Test. The magnetic beads were incubated at 37 ℃ for 8 weeks, and the antibody binding efficiency was not attenuated, which indicated that the beads had good stability.

4. Antibody elution system is closer to neutral

• This product uses an optimized elution buffer to elute antibodies at pH 4.5, greatly reducing the risk of acid-sensitive antibodies being damaged in low pH elution environments.

5. Very low protein A ligand off rate

• Protein A residues in antibody purification products for Beaver Beads ™ beads are lower than US FDA standards (20 ppm). And has been certified by the foreign well-known foreign products no significant difference.

6. Reusable

• BeaverBeads ™ antibody purified beads can be reused and regenerated, and maintain high antibody binding efficiency. After 15 uninterrupted purification operations, 75% of the lgG binding capacity was maintained, and the antibody binding capacity was restored to the original 90% after regeneration treatment.