ROTI®Garose-Protein A/G HPBeads, 1 ml

For rapid and simple purification of antibodies with reasonable effort, affinity chromatography still is the first choice in most cases. ROTI^®Garose-Protein A and G Beads offer the perfect solution for your specific application under medium pressure (MPLC, FPLC), if rapid flow rates are desired or if big samples volumes have to be purified.

The matrix of ROTI^®Garose-Protein A and G Beads consists of crosslinked and beaded 4 % agarose, coated and covalently coupled with protein A from Staphylococcus aureus and protein G from Streptococcus, respectively.
The recombinant protein A (recA) shares IgG binding properties with natural protein A of S. aureus Cowan strain I. It has high affinity for IgG from a variety of different mammalian species, also binding some populations of IgA and IgM.
Binding domains specific for albumin as well as cell walls and cell membranes have been removed in the recombinant protein G, in order to ensure the maximum specific IgG binding capacity. It has high affinity for IgG from a variety of different mammalian species, also binding IgG3 with high affinity.

Most immunoglobulins may be eluted in 100 mM glycin or citric acid buffer (pH 3.0). ROTI^®Garose-Protein A and G Beads may be regenerated, making them very cost-effective.
May not be autoclaved.

Mixture (1:1) of protein A- and protein G coated agarose beads for affinity chromatography under medium pressure, with high flow rate or with big sample-/matrix volume. High-performance affinity resin for antibody purification.
In ROTI^®Garose-Protein A/G HPBeads, the advantages of the highly efficient protein A and G/antibody binding have been combined with a bead technology allowing a very rapid flow rate.
50 % bead suspension in 20 % ethanol.

All small-scale applications, for MPLC and FPLC, or if antibodies shall be isolated either in short time or in big amounts.

The matrix of ROTI^®Garose-Protein A/G HPBeads consists of crosslinked and beaded 4 % agarose, coated and covalently coupled with protein A from Staphylococcus aureus and protein G from Streptococcus, respectively.
High binding affinity to IgGs of many different mammalian species, high affinity binding of all IgG3, binding of some populations IgA and IgM.