Core Facility Nanobodies
The Core Facility Nanobodies offers the customized generation of alpaca or llama variable domains of heavy chain-only antibodies (VHHs), also called nanobodies, against target structures of choice. We also offer the production of Nanobodies and the conjugation to biotin, fluorochromes and others.
The CFN is actively engaged in method development and part of translational resarch projects.
NANOBODY® is a registered trademark of Ablynx N.V.


Background
The Core Facility Nanobodies offers the customized generation of alpaca or llama variable domains of heavy chain-only antibodies (VHHs) against target structures of choice. These VHH domains are also called nanobodies®. These highly specific single domain antibodies recognize their targets with affinities comparable to conventional antibodies but are much smaller (ca. 15 kDa), more stable and more versatile for many applications.
NANOBODY® is a registered trademark of Ablynx N.V.

Service
The Core Facility Nanobodies offers the generation of customized nanobodies against an antigen of your choice, the production of nanobodies, basic nanobody characterization as well as conjugation of nanobodies to different dyes or molecules.

Getting started
If you are interested in raising nanobodies against specific proteins or other immunogens, please contact us through the web interface below. We can discuss the possible application of nanobodies for your research and determine which modifications or expression systems are of interest for you.
Needful Links
Düster, Robert; Anand, Kanchan; Binder, Sophie C.; Schmitz, Maximilian; Gatterdam, Karl; Fisher, Robert P.; Geyer, Matthias (2024): Structural basis of Cdk7 activation by dual T-loop phosphorylation. In: Nature communications 15 (1), S. 6597. DOI: 10.1038/s41467-024-50891-z.
Eden, Thomas; Schaffrath, Alessa Z.; Wesolowski, Janusz; Stähler, Tobias; Tode, Natalie; Richter, Nathalie et al. (2024): Generation of nanobodies from transgenic 'LamaMice' lacking an endogenous immunoglobulin repertoire. In: Nature communications 15 (1), S. 4728. DOI: 10.1038/s41467-024-48735-x.
Lorenz, Hannah; Menzel, Stephan; Roshchyna, Nataliia; Albrecht, Birte; Gebhardt, Anna Josephine; Schneider, Enja et al. (2024): ENPP1/CD203a-targeting heavy-chain antibody reveals cell-specific expression on human immune cells. In: Cellular and molecular life sciences : CMLS 82 (1), S. 6. DOI: 10.1007/s00018-024-05539-y.
Menzel, Stephan; Duan, Yinghui; Hambach, Julia; Albrecht, Birte; Wendt-Cousin, Dorte; Winzer, Riekje et al. (2024): Generation and characterization of antagonistic anti-human CD39 nanobodies. In: Frontiers in immunology 15, S. 1328306. DOI: 10.3389/fimmu.2024.1328306.
Schneberger, Niels; Hendricks, Philipp; Peter, Martin F.; Gehrke, Erik; Binder, Sophie C.; Koenig, Paul-Albert et al. (2024): Allosteric substrate release by a sialic acid TRAP transporter substrate binding protein. In: Commun Biol 7 (1), S. 1559. DOI: 10.1038/s42003-024-07263-6.
Witt, Marius; Oliveira-Ferrer, Leticia; Koch-Nolte, Friedrich; Menzel, Stephan; Hell, Louisa; Sturmheit, Tabea et al. (2024): Expression of CD39 is associated with T cell exhaustion in ovarian cancer and its blockade reverts T cell dysfunction. In: Oncoimmunology 13 (1), S. 2346359. DOI: 10.1080/2162402X.2024.2346359.
Jenster, Lea-Marie; Lange, Karl-Elmar; Normann, Sabine; vom Hemdt, Anja; Wuerth, Jennifer D.; Schiffelers, Lisa D. J. et al. (2023): P38 kinases mediate NLRP1 inflammasome activation after ribotoxic stress response and virus infection. In: The Journal of experimental medicine 220 (1). DOI: 10.1084/jem.20220837.
Tsukamoto, Yuta; Hiono, Takahiro; Yamada, Shintaro; Matsuno, Keita; Faist, Aileen; Claff, Tobias et al. (2023): Inhibition of cellular RNA methyltransferase abrogates influenza virus capping and replication. In: Science (New York, N.Y.) 379 (6632), S. 586–591. DOI: 10.1126/science.add0875.
Bertheloot, Damien; Wanderley, Carlos Ws; Schneider, Ayda H.; Schiffelers, Lisa Dj; Wuerth, Jennifer D.; Tödtmann, Jan Mp et al. (2022): Nanobodies dismantle post-pyroptotic ASC specks and counteract inflammation in vivo. In: EMBO molecular medicine 14 (6), e15415. DOI: 10.15252/emmm.202115415.
Demeules, Mélanie; Scarpitta, Allan; Hardet, Romain; Gondé, Henri; Abad, Catalina; Blandin, Marine et al. (2022): Evaluation of nanobody-based biologics targeting purinergic checkpoints in tumor models in vivo. In: Frontiers in immunology 13, S. 1012534. DOI: 10.3389/fimmu.2022.1012534.
Dhana, Ermanila; Klaus, Daniela; Böhner, Alexander; Schmidt, Florian; Vietinghoff, Sibylle von; Boor, Peter et al. (2022): Generation of an alpaca serum that induces immune-mediated crescentic glomerulonephritis in mice. In: Journal of immunological methods 507, S. 113310. DOI: 10.1016/j.jim.2022.113310.
Peter, Martin F.; Ruland, Jan A.; Depping, Peer; Schneberger, Niels; Severi, Emmanuele; Moecking, Jonas et al. (2022): Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter. In: Nat Commun 13 (1), S. 4471. DOI: 10.1038/s41467-022-31907-y.
Lab
Jan Toedmann, Tobias Reinicke
BMZ1, EG202
Venusberg-Campus 1
53127 Bonn
+49 228 287-54731
Dr. Stephan Menzel
Venusberg-Campus 1
53127 Bonn
Acknowledgements
Administration Medical Faculty
Documents
The Core Facilities thank the German Research Foundation for continuous support.
