Cell surface proteins can be specifically biotinylated, but the enrichment of biotinylated proteins is based on streptavidin beads that are used upon cell lysis and release of proteins to a buffer. I am searching for a protocol in which I can enrich for those cells prior to lysis.
The streptavidin microbeads from Miltenyi Biotec might do the job for you. I have no connection with Miltenyi, there are probably other suitable beads out there too. You will of course have to use isotonic buffers to avoid damaging the cells.
If you have biotinylated a cell suspension, there were presumably multiple lysines on the surface proteins available for biotinylation (i.e. potentially all cells tagged?) and I'm not sure how well the fractionation will work.
Hi. Perhaps you can biotinylate the proteins with biotin that has a disulfide linker. Then you can add a reducing agent to elute your cells. This paper shows one way of doing this:
Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity - PubMed (nih.gov)
Nick Gee referring to your question: Since the biotinylation is going to be done in vivo on tissue level, not all the cells might be biotinylated.
If you know someone with a fluorescence activated cell sorter (FACS), they probably already have the necessary reagents, equipment, and protocol.
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