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| Hi there, have question about publications & your experience. I'm going to purify partially purifed recombinant protein (but containing ~30% of protein contaminations) using affinity chromatography. I produced a lot of monoclonal antibody - mouse anti-myc, and my protein has Myc-Tag. Saying produced I mean collected supernatant from hybrydoma cells. The thing is to purify & bind my antibodies and (it would be great if using the same resign/column) pass my protein throuh it, hoping it will bind with antibodies. Then wash & elute it. Do u thing that sepharose with protein A will be good? Does any of u who have expereince in this experiment may discuss this idea of expriment with me? Waiting for your replay. Bres |
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| antimyc , igg , mouse , protein , purification , tag |
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