BeaverBeads™ Protein A/G Antibody Purification Kit
BeaverBeads™ Protein A/G Antibody Purification Kit
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: 30mg/mL, 2μm
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.
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
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.
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.
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.
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.
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