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Journal Article

Nanobodies: Site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation.

MPS-Authors
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Pleiner,  T.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Bates,  M.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Trakhanov,  S.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Lee,  C. T.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Schliep,  J. E.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Chug,  H.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Böhning,  M.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Görlich,  D.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

2241607.pdf
(Publisher version), 4MB

Supplementary Material (public)

2241607_Suppl.pdf
(Supplementary material), 5MB

Citation

Pleiner, T., Bates, M., Trakhanov, S., Lee, C. T., Schliep, J. E., Chug, H., et al. (2015). Nanobodies: Site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation. eLife, 4: e11349. doi:10.7554/eLife.11349.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-535B-B
Abstract
Nanobodies are single-domain antibodies of camelid origin. We generated nanobodies against the vertebrate nuclear pore complex (NPC) and used them in STORM imaging to locate individual NPC proteins with.