In my work, i am working on a serological proteomic analysis (SERPA) project, seeking for the antigens capable of eliciting immune responses. So just like any other typical gel-based proteomic experiment the extracted protein samples are separated through a 2D gel-electrophoresis. Then the resolved protein spots are electro-transferred (my transfer buffer is Towbin) to the immobilon-PSQ membrane, which is compatible with a mass spectroscopy experiment according to the manufacture description. Transfered proteome then will be blocked and incubated in primary and secondary antibody.
For identification of proteins by mass spectrometry, I would like to excise reactive proteins from membrane instead of gel!! Could you tell me glycine which is used in Towbin buffer is compatible with mass spectrometry?
Thanks Dear kroliczewski,
Do you think this table is reliable?
Do you have any experience or paper about that?
I am not sure if this answers your question, but you could always clean-up your samples using C18 ziptips and get rid of the glycine as well as any other interfering substances, so that they ionize properly in the MALDI instrument.
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