Dr. Marlitt Stech

is the acting head of the Cell-Free Protein Synthesis group together with Dr. Anne Zemella.


Scientific focus and expertise:

Academic CV
2022 Head of the Cell-Free Protein Synthesis Group, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics & Bioprocesses (IZI-BB), Potsdam-Golm, Germany
2015 - 2022

Research Associate (Post-Doc) – Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics & Bioprocesses (IZI-BB), Potsdam-Golm, Germany

2009 - 2010 Research project (University of Edinburgh, MRC Centre for Regenerative Medicine, Institute for Stem Cell Research, Biology of Reprogramming): "Generation of macrophages from induced pluripotent stem cells and secondary reprogramming"


2011 - 2015 PhD thesis in the Department of Biochemistry (University of Potsdam): "Studies on the cell-free synthesis of single-chain antibody fragments using a eukaryotic translation system"

Master thesis (Fraunhofer Institute for Biomedical Engineering (IBMT) Potsdam-Golm; Beuth University of Applied Sciences Berlin): "Cell-free synthesis of functional antibody fragments"

2008 - 2010

Biotechnology studies (Master) at the Berlin University of Applied Sciences, Berlin

2008 Bachelor thesis (Charité - University Medicine Berlin, Center for Anatomy, Institute of Cell and Neurobiology): "Generation and cloning of mutation derivatives of the mouse PRG-1 gene and their analysis in the heterologous cell culture system"
2005 - 2008 Biotechnology studies (Bachelor) at the Technical University of Applied Sciences Berlin
2005 Abitur
Prizes and Scholarships
2009 – 2010

Erasmus Scholarship

2011 Honoring outstanding graduation in the biotechnology program at Beuth University of Applied Sciences
2017 – 2019 Talenta speed-up scholarship of the Fraunhofer Gesellschaft
Society for Biochemistry and Molecular Biology e.V.

Marlitt Stech ORCID: 0000-0002-4760-9791
  • Haueis, L., Stech, M., Schneider, E., Lanz, T., Hebel, N., Zemella, A., & Kubick, S. (2023). Rapid One-Step Capturing of Native, Cell-Free Synthesized and Membrane-Embedded GLP-1R. International Journal of Molecular Sciences, 24(3). https://doi.org/10.3390/ijms24032808
  • Haueis, L., Stech, M., & Kubick, S. (2022). A Cell-free Expression Pipeline for the Generation and Functional Characterization of Nanobodies. Frontiers in Bioengineering and Biotechnology, 10, 896763. https://doi.org/10.3389/fbioe.2022.896763.
  • Krebs, S. K., Stech, M., Jorde, F., Rakotoarinoro, N., Ramm, F., Marinoff, S., Bahrke, S., Danielczyk, A., Wüstenhagen, D. A., & Kubick, S. (2022). Synthesis of an Anti-CD7 Recombinant Immunotoxin Based on PE24 in CHO and E. Coli Cell-Free Systems. International Journal of Molecular Sciences, 23(22). https://doi.org/10.3390/ijms232213697
  • Krebs, S. K.; Rakotoarinoro, N.; Stech, M.; Zemella, A.; Kubick, S. (2022). A CHO-Based Cell-Free Dual Fluorescence Reporter System for the Straightforward Assessment of Amber Suppression and scFv Functionality. Frontiers in Bioengineering and Biotechnology. https://doi.org/10.3389/fbioe.2022.873906
  • Stech, M., Rakotoarinoro, N., Teichmann, T., Zemella, A., Thoring, L., & Kubick, S. (2021). Synthesis of Fluorescently Labeled Antibodies Using Non-Canonical Amino Acids in Eukaryotic Cell-Free Systems. Methods in Molecular Biology (Clifton, N.J.), 2305, 175–190. https://doi.org/10.1007/978-1-0716-1406-8_9
  • Ramm, F., Stech, M., Zemella, A., Frentzel, H., & Kubick, S. (2021). The Pore-Forming Hemolysin BL Enterotoxin from Bacillus cereus: Subunit Interactions in Cell-Free Systems. Toxins, 13(11). https://doi.org/10.3390/toxins13110807.
  • Dondapati, S. K., Stech, M., Zemella, A., & Kubick, S. (2020). Cell-Free Protein Synthesis: A Promising Option for Future Drug Development. BioDrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy, 34(3), 327–348. https://doi.org/10.1007/s40259-020-00417-y
  • Ramm, F., Dondapati, S. K., Thoring, L., Zemella, A., Wüstenhagen, D. A., Frentzel, H., Stech, M., & Kubick, S. (2020). Mammalian cell-free protein expression promotes the functional characterization of the tripartite non-hemolytic enterotoxin from Bacillus cereus. Scientific Reports, 10(1), 2887. https://doi.org/10.1038/s41598-020-59634-8
  • Stech, M., Nikolaeva, O., Thoring, L., Stöcklein, W. F. M., Wüstenhagen, D. A., Hust, M., Dübel, S., & Kubick, S. (2017). Cell-free synthesis of functional antibodies using a coupled in vitro transcription-translation system based on CHO cell lysates. Scientific Reports, 7(1), 12030. https://doi.org/10.1038/s41598-017-12364-w
  • Thoring, L., Dondapati, S. K., Stech, M., Wüstenhagen, D. A., & Kubick, S. (2017). High-yield production of "difficult-to-express" proteins in a continuous exchange cell-free system based on CHO cell lysates. Scientific Reports, 7(1), 11710. https://doi.org/10.1038/s41598-017-12188-8
  • Sonnabend, A., Spahn, V., Stech, M., Zemella, A., Stein, C., & Kubick, S. (2017). Production of G protein-coupled receptors in an insect-based cell-free system. Biotechnology and Bioengineering, 114(10), 2328–2338. https://doi.org/10.1002/bit.26346
  • Quast, R. B., Ballion, B., Stech, M., Sonnabend, A., Varga, B. R., Wüstenhagen, D. A., Kele, P., Schiller, S. M., & Kubick, S. (2016). Cell-free synthesis of functional human epidermal growth factor receptor: Investigation of ligand-independent dimerization in Sf21 microsomal membranes using non-canonical amino acids. Scientific Reports, 6, 34048. https://doi.org/10.1038/srep34048
  • Quast, R. B., Sonnabend, A., Stech, M., Wüstenhagen, D. A., & Kubick, S. (2016). High-yield cell-free synthesis of human EGFR by IRES-mediated protein translation in a continuous exchange cell-free reaction format. Scientific Reports, 6, 30399. https://doi.org/10.1038/srep30399
  • Thoring, L., Wüstenhagen, D. A., Borowiak, M., Stech, M., Sonnabend, A., & Kubick, S. (2016). Cell-Free Systems Based on CHO Cell Lysates: Optimization Strategies, Synthesis of "Difficult-to-Express" Proteins and Future Perspectives. PloS One, 11(9), e0163670. https://doi.org/10.1371/journal.pone.0163670
  • Quast, R. B., Kortt, O., Henkel, J., Dondapati, S. K., Wüstenhagen, D. A., Stech, M., & Kubick, S. (2015). Automated production of functional membrane proteins using eukaryotic cell-free translation systems. Journal of Biotechnology, 203, 45–53. https://doi.org/10.1016/j.jbiotec.2015.03.015
  • Stech, M., & Kubick, S. (2015). Cell-Free Synthesis Meets Antibody Production: A Review. Antibodies, 4(1), 12–33. https://doi.org/10.3390/antib4010012
  • Stech, M., Quast, R. B., Sachse, R., Schulze, C., Wüstenhagen, D. A., & Kubick, S. (2014). A continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells. PloS One, 9(5), e96635. https://doi.org/10.1371/journal.pone.0096635
  • Stech, M., Brödel, A. K., Quast, R. B., Sachse, R., & Kubick, S. (2013). Cell-free systems: Functional modules for synthetic and chemical biology. Advances in Biochemical Engineering/biotechnology, 137, 67–102. https://doi.org/10.1007/10_2013_185
  • Brödel, A. K., Sonnabend, A., Roberts, L. O., Stech, M., Wüstenhagen, D. A., & Kubick, S. (2013). Ires-mediated translation of membrane proteins and glycoproteins in eukaryotic cell-free systems. PloS One, 8(12), e82234. https://doi.org/10.1371/journal.pone.0082234
  • Stech, M., Merk, H., Schenk, J. A., Stöcklein, W. F. M., Wüstenhagen, D. A., Micheel, B., Duschl, C., Bier, F. F., & Kubick, S. (2012). Production of functional antibody fragments in a vesicle-based eukaryotic cell-free translation system. Journal of Biotechnology, 164(2), 220–231. https://doi.org/10.1016/j.jbiotec.2012.08.020

STECH, MARLITT; HANACK, KATJA; MESSERSCHMIDT, KATRIN; KUBICK, STEFAN: Method for producing polyclonal antibodies using an antigenic composition comprising protein-containing membrane vesicles. PCT/EP2014/002592

STECH, MARLITT; QUAST, ROBERT; WUESTENHAGEN, DOREEN; KUBICK, STEFAN: Verfahren und Vorrichtung zur zellfreien Proteinsynthese in Gegenwart eines Caspase-Inhibitors. PCT/EP2014/002520

  • Simultaneous protein production in cell-free systems in different reaction modes, e.g. batch and dialysis mode, coupled (transcription and translation in one reaction system) and uncoupled (transcription and translation in separate reactions)
  • Development and optimization of cell-free systems (redox-optimized systems to improve disulfide bridging, post-translational modifications)
  • Development and production of recombinant antibody formats (e.g. IgG, nanobodies, scFvs) in cell-free and cell-based systems (Sf21, CHO, HEK, E. coli)
  • Design and production of "ready-to-conjugate" antibodies with position-specific incorporated non-canonical amino acids, subsequent modification of the proteins via bioorthogonal coupling reactions (Staudinger ligation, CuAAC, SPAAC, SPIEDAC, iEDDA)
  • Design, development and production of antibody-drug conjugates (ADCs) and immunotoxins
  • Comprehensive range of methods for protein characterization and functional analysis (gel electrophoresis, autoradiography, quantification, confocal microscopy, western blotting, dot blot, enzyme-linked immunosorbent assay (ELISA), surface plasmon spectroscopy (SPR))
  • Techniques for radioactive labeling of proteins in cell-free systems (14C), qualitative and quantitative analysis of proteins with radioactive isotopes (14C).
  • RNA synthesis (transcription, analysis and purification of mRNA)
  • Techniques for solubilization (e.g., using SMA copolymers) and purification of proteins (e.g., G-protein coupled receptors (GPCRs)) from membranes and their immobilization on surfaces (e.g., magnetic beads), general techniques for protein purification (His-tag, flag-tag, twin-strep-tag, protein A).
  • Cultivation of eukaryotic cells at S1 level (primary cells, cell lines), cell culture-based assays, e.g. viability assays (e.g. CellTiter-Glo® Luminescent Cell Viability Assay, MTT assay).