Glasflaschen

Protein Production & Characterization

Dr. Anja Schütz

Profil

Recombinantly produced proteins are used for a wide range of applications in life sciences. Our platform offers expertise and services for customized protein production. In addition, you can benefit from our knowledge in the biochemical and biophysical characterization of proteins.

Our mission is to enable technology development and cutting-edge research by fostering collaboration with other technology platforms and research groups. The PPC Platform offers customized protein production for various downstream applications such as:

  • Interaction studies
  • High-throughput screening campaigns
  • Tool protein production
  • Antigen/Antibody production
  • Structural biology projects
  • Biochemical & biophysical characterization

Next to customized protein production, the PPC Platform is an ideal partner to set up collaborative research projects on topics such as protein engineering and protein characterization. We have a strong interest in studying the structure-function relationship of proteins linked to human diseases. By applying various biochemical and biophysical methods, we delineate the physicochemical properties of the analyzed proteins, a prerequisite to understand their biological function.  

The PPC Platform is in close contact with other protein productions sites and partakes in international benchmarking studies initiated through the P4EU network.

Besides being an established partner for educational training of MDC-internal apprentices, the PPC Platform is recruiting bachelor and master students. In the future, we want to promote the success of interdisciplinary PhD projects by offering the possibility of co-supervision of doctoral theses. For upcoming on-site teaching events, please check our NEWS postings. 

Are you interested in a collaboration with us? We are looking forward to your inquiry!

Team

Group Leader

 

Secretariat

 

Technical Assistants

 

Alumni

We thank our former team members for their active support.

Berger, Ingrid – Technical assistant

Donath, Mandy – Bachelor student

Haake, Fabian – Bachelor student

Lenski, Ulf – Bioinformatician

Kabuß, Loreen-Claudine H. – MDC apprentice

Kuhnke, Alina – MDC apprentice

Kurths, Silke – Technical assistant

Mustroph, Mandy – MDC apprentice

Radusheva, Veselina – Master student

Rossa, Denise – MDC apprentice

Simon, Carolin – Master student

Service & Technology

The PPCP laboratory has a strong technical expertise in the area of protein biochemistry.

We have established Standard Operating Procedures (SOPs) and attach particular importance to quality control. Our philosophy is to closely cooperate and actively exchange ideas with our collaborators, since this is essential for successful cooperation.

The following services are offered by the PPC platform:

Consulting

Scientific & technical level

Molecular biology services

 

Construct design

Gene cloning

Site-directed mutagenesis

Protein production services

Small-scale expression & solubility screening

Scale-up expression

Protein purification

Protein characterization services

(1) Protein stability determination & optimization

(2) Protein-ligand interaction studies (ligand = protein, nucleic acid, small molecule)

(3) Oligomerization analysis

(4) Protein structure determination (including crystallization, X-ray data collection)

(5) Folding analysis

In case you are interested in protein-related services not explicitly listed here, please contact us.

Publications

A: Peer-reviewed publications

Q. Ming, Y. Roske, A. Schuetz, K. Walentin, I. Ibraimi, K. Schmidt-Ott, and U. Heinemann (2018) Structural Basis of Gene Regulation by the Grainyhead/CP2 Transcription Factor Family. Nucleic Acids Res., 46, 2082-2095.

S. Quosdorf, A. Schuetz*, and H. Kolodziej* (2017) Different inhibitory potency of oseltamivir carboxylate, zanamivir, and several tannins on bacterial and viral neuraminidases as assessed in a cell-free fluorescence-based enzyme inhibition assay. Molecules, 22, 1989. *shared last authorship

A. Schuetz, V. Radusheva, S.M. Krug, and U. Heinemann (2017) Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization. Ann. N. Y. Acad. Sci., 1405, 147-159.

S. Jennek, S. Mittag, J. Reiche, J.K. Westphal, S. Seelk, M.J. Dörfel, T. Pfirrmann, K. Friedrich, A. Schütz, U. Heinemann, and O. Huber (2017) Tricellulin is a target of the ubiquitin ligase Itch. Ann. N. Y. Acad. Sci., 1397, 157-168.

E. Kowenz-Leutz, A. Schuetz, Q. Liu, M. Knoblich, U. Heinemann, and A. Leutz (2016) Functional interaction of CCAAT/enhancer-binding-protein-α basic region mutants with E2F transcription factors and DNA. Biochim. Biophys. Acta (Gene Regul. Mech.), 1859, 841-847.

Y. Murakawa, M. Hinz, J. Mothes, A. Schuetz, M. Uhl, E. Wyler, T. Yasuda, G. Mastrobuoni, C. C. Friedel, L. Dölken, S. Kempa, M. Schmidt-Supprian, N. Blüthgen, R. Backofen, U. Heinemann, J. Wolf, C. Scheidereit, M. Landthaler (2015) RC3H1 post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-κB pathway. Nat. Commun., 6, 7367.

S. Wagner, A. Schütz, and J. Rademann (2015) Light-switched inhibitors of protein tyrosine phosphatase PTP1B based on phosphonocarbonyl phenylalanine as photoactive phospho-tyrosine mimetic. Bioorg. Med. Chem., 23, 2839-2847.

A. Schuetz, Y. Murakawa, E. Rosenbaum, M. Landthaler, and U. Heinemann (2014) Roquin binding to target mRNAs involves a winged helix-turn-helix motif. Nat. Commun., 5, 5701.

A. Horatscheck, S. Wagner, J. Ortwein, B.G. Kim, M. Lisurek, S. Beligny, A. Schütz, and J. Rademann (2012) Benzoylphosphonate-based photoactive phosphopeptide mimetics for modulation of protein tyrosine phosphatases and highly specific labeling of SH2 domains. Angew. Chem. Int. Ed. Engl., 51, 9441-9447.

F. Kirchner, A. Schuetz, L.-H. Boldt, K. Martens, G. Dittmar, W. Haverkamp, L. Thierfelder, U. Heinemann, and B. Gerull (2012) Molecular insights into arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 missense mutations. Circ. Cardiovasc. Genet., 5, 400-411.

F. Mayr, A. Schütz, N. Döge, and U. Heinemann (2012) The Lin28 cold shock domain remodels the terminal loop of pre-let-7 microRNA. Nucleic Acids Res., 40, 7492-7506.

J. Hanna, A. Schütz, F. Zimmermann, J. Behlke, T. Sommer, and U. Heinemann (2012) Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex. J. Biol. Chem., 287, 8633-8640.

B. von Eyss, J. Maaskola, S. Memczak, K. Möllmann, A. Schuetz, C. Loddenkemper, M.-D. Tanh, A. Otto, K. Muegge, U. Heinemann, N. Rajewsky, and U. Ziebold (2012) The SNF2-like helicase HELLS mediates E2F3-dependent transcription and cellular transformation. EMBO J., 31, 972-985.

D. Busso, Y. Peleg, T. Heidebrecht, C. Romier, Y. Jacobovitch, A. Dantes, L. Salim, E. Troesch, A. Schuetz, U. Heinemann, G.E. Folkers, A. Geerlof, M. Wilmanns, A. Polewacz, C. Quedenau, K. Buessow, R. Adamson, E. Blagova, J. Walton, J.L. Cartwright, L.E. Bird, R.J. Owens, N.S. Berrow, K.S. Wilson, J.L. Sussman, A. Perrakis, and P.H. Celie (2011) Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study. J. Struct. Biol., 175, 159-170.

A. Schuetz, D. Nana, C. Rose, G. Zocher, M. Milanovic, J. Königsmann, R. Blasig, U. Heinemann, and D. Carstanjen (2011) The structure of the Klf4 DNA-binding domain links to self-renewal and macrophage differentiation. Cell. Mol. Life Sci., 68, 3121-3131.

K. Zaragoza, V. Bégay, A. Schuetz, U. Heinemann, and A. Leutz (2010) Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes. Mol. Cell Biol., 30, 2293-2304.

S.C. Horn, J. Hanna, C., C. Volkwein, A. Schütz, U. Heinemann, T. Sommer, and E. Jarosch (2009) Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Mol. Cell, 36, 782-793.

U.-P. Guenther, L. Handoko, R. Varon, U. Stephani, C.-Y. Tsao, J.R. Mendell, S. Lützkendorf, C. Hübner, K. von Au, S. Jablonka, G. Dittmar, U. Heinemann, A. Schuetz*, and M. Schuelke* (2009) Clinical variability in distal spinal muscular atrophy type 1 (DSMA1): determination of steady-state IGHMBP2 protein levels in five patients with infantile and juvenile disease. J. Mol. Med., 87, 31-41. *shared corresponding authorship

S. Gräslund et al. (2008) Protein production and purification. Nat. Methods, 5, 135-146.

 

B: Acknowledgements

H. Behrmann, A. Lürick, A. Kuhlee, H.K. Balderhaar, C. Bröcker, D. Kümmel, S. Engelbrecht-Vandré, U. Gohlke, S. Raunser, U. Heinemann, and C. Ungermann  (2014) Structural identification of the Vps18 β-propeller reveals a critical role in the HOPS complex stability and function. J. Biol. Chem., 289, 33503-33512.

F. Mayr, and U. Heinemann (2013) Mechanisms of Lin28-mediated miRNA and mRNA regulation – a structural and functional perspective. Int. J. Mol. Sci., 14, 16532-16553.

S. Boivin, and D.J. Hart (2011) Interaction of the influenza A virus polymerase PB2 C-terminal region with importin alpha isoforms provides insights into host adaptation and polymerase assembly. J. Biol. Chem., 286, 10439-10448.

H. Striegl, M.A. Andrade-Navarro, and U. Heinemann (2010) Armadillo motifs involved in vesicular transport. PLoS One, 5, e8991.

C: Structure Gallery

Below, you find our crystal structure depositions into the Protein Data Bank.

6EKU, 6EKS, 5N7H, 5N7I, 5N7K, 5MR7, 5MPH, 5MPI, 5MPF, 4ULW, 3ZM0, 3ZM1, 3ZM2, 3ZM3, 4A75, 4A76, 4ALP, 3ULJ, 4A4I, 3TT9, 2YMA, 2WBS, 2WBU

D: Patents

M. Bader, E. Specker, S. Matthes, A. Schütz, K. Mallow, M. Grohmann, M. Nazaré. Xanthine derivatives, their use as a medicament, and pharmaceutical preparations comprising the same. Europe Patent WO/2018/019917 filed 28 Jul 2016, and issued 1 Feb 2018.

M. Bader, E. Specker, S. Matthes, A. Schütz, K. Mallow, M. Grohmann, M. Nazaré. Xanthine derivatives, their use as a medicament, and pharmaceutical preparations comprising the same. Europe Patent WO/2016/135199 filed 24 Feb. 2015, and issued 1 Sept. 2016.

Dr. Anja Schütz
Dr. Anja Schütz
Contact
Phone: 9406-2985
Max-Delbrück-Centrum für Molekulare Medizin (MDC)
Robert-Rössle-Str. 10
13092 Berlin, Deutschland
Building 87, Room 3.13