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Hi, everyone~
I met some confusion nowadays. In my ChIP-SEQ assay, the quanlity of DNA fragments of MOCK control is as same as the the one added Ab.
I have tried switch to high salt wash buffer, and more times wash, and also tried to conjuction antibody to beads first. And I even attempted to use low pH Glycine solutin to elute the antibody. But totally workless.
I'm sure that my interested protein was immoprecipiated after western blot.
So, I'm so curious that why the Mock and the Ab Group share the same DNA quanlity?
The antibody I used was Anti-myc(9E10),bought form Sigma. My interseted protein was added with 18-myc tag. And I do my ChIP assay with Separose bead protein G.
I was told that dynabead proterin G from invitrogen will give me much reduced background, is this true?
I met some confusion nowadays. In my ChIP-SEQ assay, the quanlity of DNA fragments of MOCK control is as same as the the one added Ab.
I have tried switch to high salt wash buffer, and more times wash, and also tried to conjuction antibody to beads first. And I even attempted to use low pH Glycine solutin to elute the antibody. But totally workless.
I'm sure that my interested protein was immoprecipiated after western blot.
So, I'm so curious that why the Mock and the Ab Group share the same DNA quanlity?
The antibody I used was Anti-myc(9E10),bought form Sigma. My interseted protein was added with 18-myc tag. And I do my ChIP assay with Separose bead protein G.
I was told that dynabead proterin G from invitrogen will give me much reduced background, is this true?
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