Bialon, M.M.BialonGrezella, C.C.GrezellaFriesen, L.L.FriesenSieben, T.T.SiebenPham, A.-T.A.-T.PhamFischer, R.R.FischerBarth, S.S.BarthPüttmann, C.C.PüttmannStein, C.C.Stein2022-03-052022-03-052016https://publica.fraunhofer.de/handle/publica/24608710.1089/mab.2016.0002SNAP-tag technology allows recombinant proteins to be covalently labeled to O6-benzylguanine (BG)-modified substrates with 1:1 stoichiometry. By attaching according fluorophores, this method is ideally suited for in vitro and in vivo imaging, as well as protein interaction analyses. Fluorophores modified with BG react with the SNAP-tag, whereas those modified with O2-benzylcytosine (BC) conjugate to a more recent derivative known as the CLIP-tag. The orthogonal substrate specificity of the SNAP- and CLIP-tags extends the range of applications by allowing double labeling. We previously developed a monoclonal antibody (mAb) that recognizes both tags. In this study, we describe a new mAb, which is specific for the SNAP-tag alone. Therefore, this mAb allows discrimination between SNAP- and CLIP-tags within a broad range of immunological methods, including enzyme-linked immunosorbent assays, western blotting, flow cytometry, and immunohistochemistry.en572journal article