Recombinant Protein A/G (r-PAG)

Recombinant protein to protein G fusion protein (r-page) fused 8 Fc-binding regions of the antibody, including 5 Fc-binding domains of Staphylococcus aureus protein A and 3 Fc-binding domains of the G protein of Staphylococcus aureus. Streptococcus, and removed the cell wall-binding domain, the albumin-binding domain, and the non-specific binding domain of protein A and protein G. Compared to a single protein A or protein G, it has a range broadest binding and can bind to all subtypes of human IgG.

IgA, IgE, and IgM, but not mouse serum IgA, IgM, and albumin. It is suitable for the extraction and detection of mouse IgG monoclonal antibodies. At the same time, the fused r-page reduced the pH dependence and allowed binding at pH 5-8.

Recombinant proteins expressed in the mammalian systems have a profound impact in many areas of basic and applied research, as well as the biotech/biopharma companies. For biotech/biopharma companies, they have heavily invested in the production of protein therapeutics as a relatively new and transformative approach to treating human diseases.

For academic research groups, recombinant mammalian proteins will be required for functional and high-resolution structure determination. By far the greatest demand for recombinant mammalian proteins is for therapeutic development and applications.

BioIntron recombinant protein expression platform can provide high-quality protein in a flexible, cost-effective manner, in the least amount of time.

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