Plateforme de spectrométrie de masse
Spectrométrie de masse
La plateforme offre une expertise en spectrométrie de masse et peut assister les scientifiques dans leurs analyses protéomiques, qu’il s’agisse de protéines purifiées ou d’échantillons protéiques complexes.
Nos services vont du simple contrôle de qualité des protéines recombinantes et de l’identification des protéines à la quantification relative des protéomes et à la caractérisation des modifications post-traductionnelles.
La plateforme réalise régulièrement des expériences de quantification sans marquage, mais aussi des analyses de quantification relative après marquage chimique ou métabolique (p. ex. SILAC). Les analyses de données sont effectuées avec les logiciels MaxQuant/Perseus ou ProteomeDiscoverer. Selon la nature de l’analyse, l’échantillon fourni sera sous forme liquide ou dérivé d’un gel SDS-PAGE. Nous pouvons également conseiller et former les chercheurs et les étudiants à la préparation des échantillons et à l’analyse des résultats.
Contact
Responsable scientifique
Christophe MARCHAND
IR CNRS – UMR 8226
Ingénieur plateforme
Marion HAMON
IE CNRS – FR 550
Mail : proteomics@ibpc.fr
Actualités
Poster : Proteomic Platform (IBPC) : a mass spectrometry facility open to the scientific community
Equipements
La plateforme est équipée de deux spectromètres de masse : un MALDI-TOF/TOF Axima Performance (Shimadzu) et un système d’électrospray Q-Exactive plus couplé à un système de chromatographie liquide à ultra-haute performance Vanquish Neo nano-flow acquis en 2023 (Thermofisher Scientific), ainsi qu’un système HPLC conventionnel (détecteurs UV et DAD).
Système HPLC permettant une chromatographie préparative et analytique.
Spectromètre de masse en tandem neuf à très haute résolution Q Exactive (Thermoscientific) couplé en amont à une nano-chromatographie liquide à ultra haute performance Nano Easy1000 (Thermoscientific).
Spectromètre de masse MALDI-TOF/TOF Axima Performance (Shimadzu)
Réservation
Interne IBPC
Un planning de réservation du MALDI-TOF est désormais disponible en ligne pour le personnel formé de l’IBPC. Pensez à réserver.
https://resa-equipement.ibpc.fr/
Externe IBPC
Pour toute demande de réservation externe à l’IBPC, ou pour toute demande de formation contacter :
Analyses
La plateforme propose différents types d’analyses :
- Préparation d’échantillon Digestion gel d’électrophorèse (spot ou bande)
- Digestion en solution
- Purification de peptides C18
- Identification de protéines purifiées
(mélange peptidique simple) - Identification de protéines en mélange complexe (séparation chromatographique préalable)
- Mesure de masse sur protéine entière
(en solution) - Protéomique quantitative : développement de techniques type label free
Des protocoles sont disponibles ci-dessous mais une prise de contact avec le plateau est recommandée avant toute préparation d’échantillon.
Pour toute demande d’analyse contacter : proteomics@ibpc.fr
Remerciements & Tarification
Avec la diversité de la plateforme, trois grilles tarifaires ont été établies selon la décision tarifaire DEC247241DR02 :
– Maldi-TOF ;
– préparation des échantillons ;
– analyse Qexactive.
| Type d’analyse |
Facturation interne- clients partenaires |
Clients externes académiques |
Clients privés |
|---|---|---|---|
|
Analyse MALDI-TOF |
14.38 € |
62.26 € |
90.04 € |
|
Préparation d’échantillon |
1.37 € |
43.56 € |
56.63 € |
|
Analyse Q-Exactive |
96.10 € |
299.65 € |
389.55 € |
Merci aux utilisateurs de la plateforme d’inclure pour toute publication utilisant des résultats acquis grâce à la plateforme de protéomique de l’IBPC la phrase suivante :
The authors acknowledge access to the proteomic platform of the IBPC that is supported by the CNRS, the Labex DYNAMO (ANR-11-LABX-0011), the Equipex CACSICE (ANR-11-EQPX-0008) and the CPER PSLRESOLUTION.
Label
La plateforme est labellisé IBiSA depuis janvier 2025.
Actualités de la plateforme
Les plateformes de l’IBPC sont référencées sur le site du GIS IBiSA
Les plateformes de l’IBPC ont reçu le label IBisA depuis le 1er janvier 2025. Source Photo : microcalorimètre ITC (plateforme de biophysique) Les plateformes
28 juillet 2025
Les plateformes présentes à la première journée scientifique de l’Institut de Chimie Biologique (4 avril 2025)
Les plateformes de l’IBPC ont participé à l’événement en présentant un poster. Les plateformes de l’IBPC ont présenté les instruments et l’expertise développé eu
10 avril 2025
Convergences première journée Institut Pasteur – Université Paris Cité (17 juin 2024)
À l’occasion de l’événement, les plateformes de l’IBPC ont présenté un poster illustrant leurs activités. Le programme de cette journée a permis de voir l’évolution
17 juin 2024
Liste de publications
5511665
82TPS5CH
Mass_plateforme
1
apa
50
date
desc
year
2071
http://www.ibpcwp.ibpc.fr/wp-content/plugins/zotpress/
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de Carpentier, F., Maes, A., Marchand, C. H., Chung, C., Durand, C., Crozet, P., Lemaire, S. D., & Danon, A. (2022). How abiotic stress-induced socialization leads to the formation of massive aggregates in Chlamydomonas. Plant Physiology, 190(3), 1927–1940. https://doi.org/10.1093/plphys/kiac321
Mattioli, E. J., Rossi, J., Meloni, M., De Mia, M., Marchand, C. H., Tagliani, A., Fanti, S., Falini, G., Trost, P., Lemaire, S. D., Fermani, S., Calvaresi, M., & Zaffagnini, M. (2022). Structural snapshots of nitrosoglutathione binding and reactivity underlying S-nitrosylation of photosynthetic GAPDH. Redox Biology, 54, 102387. https://doi.org/10.1016/j.redox.2022.102387
Borde, C., Dillard, C., L’Honoré, A., Quignon, F., Hamon, M., Marchand, C. H., Faccion, R. S., Costa, M. G. S., Pramil, E., Larsen, A. K., Sabbah, M., Lemaire, S. D., Maréchal, V., & Escargueil, A. E. (2022). The C-Terminal Acidic Tail Modulates the Anticancer Properties of HMGB1. International Journal of Molecular Sciences, 23(14), 7865. https://doi.org/10.3390/ijms23147865
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Martins, L., Knuesting, J., Bariat, L., Dard, A., Freibert, S. A., Marchand, C., Young, D., Dung, N. H. T., Voth, W., Bures, A. de, Saez-Vasquez, J., Lemaire, S. D., Roland, L., Messens, J., Scheibe, R., Reichheld, J.-P., & Riondet, C. (2020). Redox modification of the Fe-S glutaredoxin GRXS17 activates holdase activity and protects plants from heat stress. Plant Physiology. https://doi.org/10.1104/pp.20.00906
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Shao, Z., Borde, C., Marchand, C. H., Lemaire, S. D., Busson, P., Gozlan, J.-M., Escargueil, A., & Maréchal, V. (2019). Detection of IgG directed against a recombinant form of Epstein-Barr virus BALF0/1 protein in patients with nasopharyngeal carcinoma. Protein Expression and Purification, 162, 44–50. https://doi.org/10.1016/j.pep.2019.05.010
Dautant, A., Henri, J., Wales, T. E., Meyer, P., Engen, J. R., & Georgescauld, F. (2019). Remodeling of the Binding Site of Nucleoside Diphosphate Kinase Revealed by X-ray Structure and H/D Exchange. Biochemistry, 58(10), 1440–1449. https://doi.org/10.1021/acs.biochem.8b01308
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Berger, H., De Mia, M., Morisse, S., Marchand, C. H., Lemaire, S. D., Wobbe, L., & Kruse, O. (2016). A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. Plant Physiology, 171(2), 821–832. https://doi.org/10.1104/pp.15.01878