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CaptureSelect™ IgG-Fc (ms) PhyTip columns for purification of IgGs
CaptureSelect™ IgG-Fc (ms) is used for purification of IgGs in various species by binding to the Fc region of IgG antibodies. This affinity media was designed to purity IgGs from multiple species including mouse, cow, rabbit, rat, goat, horse, human and sheep. CaptureSelect™ IgG-Fc (ms) bind at a highly conserved epitope on the Fc region of the heavy chain. Unlike protein G, which under standard elution conditions is known to present challenges that result in poor yield, dissociated homodimers and denatured antibodies, this product can be used with gentle elution conditions for retained structural and functional integrity of the purified protein.
The affinity ligands of CaptureSelect™ medias from ThermoFisher are based on a recombinant antibody fragment of only 14 kDa in size that can be adapted for highly selective binding to certain parts or antibodies and antibody fragments.
PhyNexus, now part of Biotage, developed the PhyTip® column in 2002 and have supported researchers with automated protein purification ever since. PhyTip columns purify samples by repeated back-and-forth cycles - a process called dual flow chromatography which allows complete binding interactions in each purification step.
Due to maximization of binding of the sample, less protein is lost during the purification process. The result is very high sample recoveries.
Our unique column design with a packed resin bed results in binding of the entire sample to a small resin bed volume. The purified sample can be eluted in small volumes, resulting in a highly concentrated sample.
Effective purification by PhyTip columns enables a full purification protocol of 96 samples in as little as 15 minutes.
Our PhyTip columns are available for all major liquid handling platforms to enable you to use your existing system that you may already have in your lab for automated protein purification. If you don't have a system, we offer automation solutions for protein purification by PhyTip columns.
