The Molecular Immunology Hub encompasses a diverse range of state of the art instrumentation and expertise for the generation of nanobodies and monoclonal antibodies, and houses highly advanced technologies for the analysis of proteins, biomolecules and metabolites.
The facility houses an excellent array of state-of-the-art mass spectrometers (Orbitrap, Q-ToF’s, MALDI ToF-ToF, ion trap, ESI-ToF), combined with extensive protein and peptide separation methods (2D-gel, DiGE, HPLC, nano-HPLC, chip-based ESI, chip-based LC, SPR, LC-MALDI, scanners) and focuses on the development of innovative proteomics techniques to improve protein expression quantification, the analysis of membrane proteins, protein post-translational modifications, protein network and alternative protein and peptide separation methods.
This world-renowned group has expertise in Native MS, an analytical technique that allows the mass spectrometric analysis of intact proteins and protein complexes under their native folded state. The key feature that makes native MS unique is the retention of molecular non-covalent interactions during the ionization process and the subsequent mass analysis.
The facility has a dedicated service unit (Ablab) that provides commercial access to state of the art native mass spectrometry (MS) services. Please contact the Utrecht Life Sciences Ablab facility website for procedures for access to the facility.
The facility also coordinates the current EU funded EPIC-XS project, a consortium that provides access to leading proteomics facilities and research groups in Europe, .
For more information, procedures for access to the facility and for contact details, please visit the website of the mass spectrometry facility:
The facilty for electron microscopy is hosted by the Cryo-EM group and is devoted to the development and application of technologies for (cryo) specimen preparation, 3D (cryo) electron microscopy data collection, as well as image analysis for cell biology and material sciences applications.
For life science research the facility offers the tools and technical expertise for the preparation of biological specimens with perservation of ultrastructures (including cyro-fixation, freeze substitution, and high pressure freezing of samples, immunolabeling, serial sectioning and high resolution electron tomography to study 3D structure of cells tissues and protein complexes.
The lab operates 6 electron microscopes (2 scanning and 4 transmission electron microscopes) and the ancillary equipment needed for preparation of specimens (either from material sciences, geology, medicine or biology) for EM and other microscopy.
The infrastructure includes several traditional Transmission Electron Microscopes (TEMs) and a Scanning Electron Microscopes (SEM), both with a full range of attachments such as STEM, EDX and energy-filtering. In addition it houses a specialised Focussed Ion Beam-SEM and an Integrated Light Electron Microscope (ILEM).The group houses the equipment to prepare specimen with preservation of ultrastructure (including cryo-fixation and freeze-substitution of samples), immunolabeling, serial-sectioning and high-resolution electron tomography and Slice and View to study three dimensional structure of cells, tissues and other materials.
The National Single Crystal X-ray Facility in the Crystal and Structural Chemistry group offers crystal structure determinations to synthetic chemists at universities, institutes and companies in The Netherlands. With experienced staff, state-of-the-art equipment and advanced software we are able to handle a large variation of chemical compounds.
In academic collaborations we contribute significantly to the preparation of scientific publications. Examples of our structural studies include model systems that mimic catalytic sites in proteins or synthetic catalysts to be used in the clean production of desired pharmaceuticals or materials. Such studies are necessary for a detailed understanding of the catalytic process at the molecular level. Similarly, crystal structures of pharmaceuticals are studied to obtain experimental evidence of molecular conformations, intermolecular interactions, absolute configuration, polymorphs and details of solvent inclusions. This information is needed as guidance to develop better pharmaceuticals. Supramolecular structures of self-organizing molecules through intermolecular interactions are studied as part of research aiming at the development of desired new materials.
The SON NMR Large-Scale Facility provides access to state-of-the-art solution state as well as solid state NMR equipment to both Dutch and international researchers. In addition to the NMR machine park, SONNMRLSF harbors an extensive computational infrastructure for Molecular Modelling, NMR structure calculations and docking simulations. The facility can also provide advanced training of young scientists.
The solution state NMR infrastructure of the NMR spectroscopy at the Bijvoet Center of Utrecht University group consists of a 900 MHz, a 750 MHz and two 600 MHz NMR spectrometers completely up to date with respect to current and future needs of high resolution NMR. The 900 and one of the 600 MHz spectrometers are equipped with cryprobe systems for enhanced sensitivity. One of the 500 MHz spectrometers is equipped with a laser system for light-related NMR experiments. A second laser (Argon-laser) is present, for example, for CIDNP-related NMR experiments. The solid state NMR the infrastructure of the NMR spectroscopy group at the Bijvoet Center of Utrecht University has a 500 MHz wide-bore, a 700 MHz narrow-bore spectrometer and 400 MHz and 800MHz narrow bore spectrometers with the possibility to perform DNP experiments. The facility will also host a new 950 Mhz and eventually 1.2 GHz NMR spectrometer as part of the uNMR-NL NWO Roadmap project. Developed by the NMR spectroscopy group at the Bijvoet Center of Utrecht University, several web portals provide access to powerful software packages ported. A wide range of structural biology related software packages are available covering the many stages in NMR structure calculation, molecular dynamics simulations and structure modelling.
For more information, procedures for access to the facility and for contact details, please visit the Utrecht Life Science NMR facilities website .
The Biomolecular Interaction Facility offers label free analysis of biomolecular interactions using biolayer interferometry and isothermal titration calorimetry.
It is an optical analytical technique that analyses the interference pattern of white light reflected from two surfaces: a layer of immobilised protein on the biosensor tip, and an internal reference layer. Any change in the number of molecules bound to the biosensor tip causes a shift in the interference pattern that can be measured in real-time. Simple dip and read measurements can be used to perform in-depth kinetic analysis of biomolecular interactions, to determine the amount of biomolecules present in solution, to develop assays and to perform diverse screening applications. A wide range of biosensors are making this system very flexible in application.
This facility offers a wide range of techniques and expertise for the generation of monoclonal antibodies required for immunotherapy. The facility offers:
Immunization of mice, wild type or knock out
Screening of serum titers
Generation and screening of hybridoma’s
New Immunization method
A new and very efficient cellular immunization method is also available. With this method, antibodies can be raised against low immunogenic membrane proteins, such as multispanning membrane proteins, conformational epitopes and we can generate agonistic and antagonistic mABs. On request we can make mABs against soluble proteins/peptides with Complete Freund’s adjuvant.
Dossier management for ethical approval (Animal Experiments Committee)
Handling of mice
Collecting spleen of positive mice
Fusion of spleen cells to generate hybridoma’s
Selection of positive hybridoma’s
Long term storage
Extra services such as antibody purification on request.
For more information, procedures for access to the facility and for contact details, please visit the Utrecht Life Science Utrecht Monoclonal Antobody Facility.
Celia Berkers (Institute for Chemical Immunology researcher) is the newly appointed Professor of Metabolomics at the Faculty of Veterinary Medicine and Science (Department of Chemistry).
Professor Berkers will mainly focus on metabolism research in order to better understand the role of metabolic processes in health and disease.
For more information, procedures for access to the facility and for contact details, please contact Celia Berkers.
Animals of the camelidae family have next to their repertoire of conventional antibodies also smaller antibodies, which are composed of heavy chain only and are devoid of light chains. These unusual small sized antibodies can be further reduced in size in absence of the Fc region. This structure is called single domain antibody (sdAb), variable domain of the heavy chain antibody (VHH) or nanobody. Nanobodies belong to the smallest functional antigen binding fragments (around 15 kDa), which are only one tenth the size of a conventional antibody.
The nanobody facility is experienced in further functionalization of nanobodies (which have been selected using phage display technology) using different conjugation strategies including sortase tagging and click-chemistry. Examples exist for application of different nanobody conjugates for superresolution light microcopy, electron microcopy, and for development of novel diagnostic and therapeutic approaches including targeted nanoparticles and photodynamic therapy.
For more information, procedures for access to the facility and for contact details, please visit the Utrecht Life Science Utrecht Nanobody Facility.
The mission of the Tumor Immunology Facility at the University Medical center Utrecht (UMCU) concerns the development and clinical application of innovative treatment strategies toward improving the outcome of hematological cancers and treatment associated (chronic) complications.To unravel mechanisms how the human immune system protects us from developing cancer provides the key for novel therapies and generates most promising remedies for patients suffering from malignancies.
To accomplish our mission, the research activities of the section applied / tumor immunology are concentrated in five fields of innovation: