Protein production and purification facility

Leader: Nicolas BAUMBERGER

Description

 

In order to address properly many biological questions one needs to dispose of sufficient amount of pure, homogenous and functional proteins. Several heterologous expression systems of pro– and eukaryotic origin have been developed over the years and can be used together with recombinant DNA technologies to fulfil this objective.

The p3P facility is a specialized service which provides practical and technological support to research groups in order to ease and accelerate the production and purification of recombinant proteins, whichever their final use (immunization, enzymatic test, interaction assay, structural studies).

In that perspective, the facility manages and distributes collections of strains, cell lines, and vectors for heterologous protein expression in various systems. It also centralizes diverse dedicated equipment for cells cultivation, cell disruption, and protein chromatography, while ensuring their maintenance and training potential users. It also offers expertise in the design and execution of experiments or alternatively, produces and purifies proteins on behalf of research team. Finally it carries a scientific and technological watch, test and set up locally developments deemed useful for the IBMP community.

Expertises

Providing material and informations

Establishing collections of vectors (especially Gateway compatible) and bacterial strains for recombinant protein expression in prokaryotic cells, distributing expression plasmids, competent cells, proteases, enzymes for molecular biology (Taq polymerase), offering tools for difficult to express proteins (chaperons), providing reagents for protein purification (metal chelating resins) and 2D-electrophoresis, providing protocols, training and assistance in planning expression or purification strategies, as well as assistance during work

Management and maintenance of the equipments

  • Bacterial cultures orbital incubators and accessories (baffled flasks, 24xdeepwell plates), laminar flow
  • Cell disruption (sonicator)
  • Chromatography systems and columns (Ion exchange, gel filtration, affinity…)

Members

Recent publications

  • MÉTEIGNIER L.V., GHANDOUR R., MEIERHOFF K., ZIMMERMANN A., CHICHER J., BAUMBERGER N., ALIOUA A., MEURER J., ZOSCHKE R. and HAMMANI K.

    The Arabidopsis mTERF-repeat MDA1 protein plays a dual function in transcription and stabilization of specific chloroplast transcripts within the psbE and ndhH operons

    New Phytologist, :, 2020. | DOI : doi.org/10.1111/nph.16625DOI logo

  • HAZMAN M., SÜHNEL M., SCHÄFER S., ZUMSTEG J., LESOT A., BELTRAN F., MARQUIS V., HERRGOTT L., MIESCH L., RIEMANN M. and HEITZ T.

    Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress

    Rice, :45, 2019. | DOI : 10.1186/s12284-019-0303-0DOI logo

  • DERRIEN B., CLAVEL M., BAUMBERGER N., IKI T., SARAZIN A., HACQUARD T., ZIEGLER-GRAFF V., VAUCHERET H., MICOL J.L., VOINNET O. and GENSCHIK P.

    A Suppressor Screen for AGO1 Degradation by the Viral F-Box P0 Protein Uncovers a Role for AGO DUF1785 in sRNA Duplex Unwinding.

    Plant Cell, :1353-1374., 2018. | DOI : 10.1105/tpc.18.00111DOI logo

  • DUBOIS M., SELDEN K., BEDIEE A., ROLLAND G., BAUMBERGER N., NOIR S., BACH L., LAMY G., GRANIER C. and GENSCHIK P.

    SIAMESE-RELATED1 Is Regulated Posttranslationally and Participates in Repression of Leaf Growth under Moderate Drought.

    Plant Physiology, :2834-2850, 2018.

  • FELIPO BENAVENT A., URBEZ C., BLANCO-TOURINAN N., SERRANO-MISLATA A., BAUMBERGER N., ACHARD P., AGUSTI J., BLAZQUEZ M.A. and ALABADI D.

    Regulation of xylem fibers differentiation by gibberellins through DELLA-KNAT1 interaction

    Development, 145:145: dev164962, 2018. | DOI : 10.1242/dev.164962DOI logo