Remigiusz Serwa, PhD
ORCID: 0000-0002-4684-3754
PROTEOMICS CORE FACILITY
proteomics@imol.institute
+48 532-823-156
- About
- members of the group
- Publications
- Equipment
- REGULATIONS
- PRICE LIST
- Chemical proteomics platform price list
- ORDER FORM
About
The IMol Proteomics Core Facility is a specialized laboratory focused on the analysis of complex peptide and protein mixtures. We provide end-to-end support – from experimental design and sample preparation to LC-MS/MS measurements, data analysis, and data mining – for both internal and external users. Explore our service portfolio – see the Price List.
Chemical Proteomics Platform
At the Chemical Proteomics Platform, we drive innovation in drug development by expanding our library of chemical tools (e.g., molecular probes that react selectively with defined amino-acid residues) alongside a portfolio of tool-free approaches (e.g., the proteome integral solubility assay, PISA). Together, these complementary strategies enable the discovery and mapping of interactions between small molecules (e.g., metabolites, cofactors, post-translational modifiers, natural products, approved medicines, and drug candidates) and proteins in living cells, whole organisms, or disease models. These efforts power an increasingly effective chemical proteomics platform that applies at least two orthogonal methodologies to identify small-molecule-binding proteins and pinpoint their binding sites – ultimately addressing the needs of scientists, biotech companies, and the broader society. We offer advanced services for both academic and business users, accelerating drug development and supporting small-molecule research. For detailed information about available services and pricing, please refer to the Chemical Proteomics Platform Price List.
Dr. Remigiusz Serwa’s team explores chemical biology with a focus on polyamine-protein interactions. Polyamines are ubiquitous small molecules essential for key physiological processes, and their dysregulation is linked to diseases such as cancer, neurodegenerative, and psychiatric disorders. The group develops and applies molecular probes for proteomics-driven, system-wide studies of the biological networks underlying these interactions. This research is supported by the National Science Centre (NCN), Poland – Sonata Bis 10 (2020/38/E/ST4/00250).
Members of the group
| Name | Surname | Degree | |||||
| Magdalena | Chojnacka | PhD | m.chojnacka@imol.institute | ||||
| Agata | Pytyś | a.pytys@imol.institute | |||||
| Zuzanna | Sas | PhD | z.sas@imol.institute | ||||
| Remigiusz | Serwa | PhD | r.serwa@imol.institute | ||||
| Former memebers | |||||||
| Viktoriia | Lastivka | v.lastivka@imol.institute | |||||
| Maciej | Zakrzewski | PhD | m.zakrzewski@imol.institute |
- Pytyś, A., Ijaz, R., Buszka, A., Miłek, J., Figiel, I., Wardaszka-Pianka, P., Roszkowska, M., Mierzwa, N., Wojtas, A., Kerstein, E., Serwa, R., Kalita, K., Dzakpasu, R., Dziembowska, M., Włodarczyk, J., & Wójtowicz, T. (2025). Temporal and protein-specific S-palmitoylation supports synaptic and neural network plasticity. Cellular and molecular life sciences : CMLS, 82(1), 355. https://doi.org/10.1007/s00018-025-05893-5
- Zakrzewski, M., Sas, Z., Cocom-Chan, B., Firdaus, M. E. R., Kałek, M., Szczepanowska, K., Gerlach, P., Marusiak, A., & Serwa, R. A. (2025). Profiling polyamine-protein interactions in live cells through photoaffinity labeling. RSC chemical biology, 10.1039/d5cb00103j. Advance online publication. https://doi.org/10.1039/d5cb00103j
- Wasilewski, M., Mohanraj, K., Zakrzewski, M., Serwa, R. A., & Chacinska, A. (2025). MitoRUSH as a tool to study the efficiency of mitochondrial import in complex I-deficient cells. Journal of cell science, 138(13), jcs263701. https://doi.org/10.1242/jcs.263701
- Katerji, M., Bergman, K. L., Lindberg, E., Rubin, M. R., Funk, A. L., Woodroofe, C. C., Nyswaner, K., Karpińska, K., Serwa, R., Marusiak, A., Swenson, R. E., & Brognard, J. F. (2025). Discovery of potent and selective PROTACs for the protein kinase LZK for the treatment of head and neck cancer. The Journal of biological chemistry, 108452. https://doi.org/10.1016/j.jbc.2025.108452
- Thapa, P., Chikale, R. V., Szulc, N. A., Pandrea, M. T., Sztyler, A., Jaggi, K., Niklewicz, M., Serwa, R. A., Hoppe, T., & Pokrzywa, W. (2024). HSP70 inhibits CHIP E3 ligase activity to maintain germline function in Caenorhabditis elegans. The Journal of biological chemistry, 107864. Advance online publication. https://doi.org/10.1016/j.jbc.2024.107864
- Kulma, M., Hofman, B., Szostakowska-Rodzoś, M., Dymkowska, D., Serwa, R., Piwowar, K., Belczyk-Ciesielska, A., Grochowska, J., Tuszyńska, I., Muchowicz, A., Drzewicka, K., Zabłocki, K., & Zasłona, Z. (2024). The ubiquitin-specific protease 21 is critical for cancer cell mitochondrial function and regulates proliferation and migration. The Journal of biological chemistry, 107793. Advance online publication. https://doi.org/10.1016/j.jbc.2024.107793
- Stępkowski, T. M., Linke, V., Stadnik, D., Zakrzewski, M., Zawada, A. E., Serwa, R. A., & Chacinska, A. (2024). Temporal alterations of the nascent proteome in response to mitochondrial stress. Cell reports, 43(10), 114803. Advance online publication. https://doi.org/10.1016/j.celrep.2024.114803
- Karpińska, K., Mehlich, D., Sabbasani, V. R., Łomiak, M., Torres-Ayuso, P., Wróbel, K., Truong, V. N., Serwa, R., Swenson, R. E., Brognard, J., & Marusiak, A. A. (2024). Selective Degradation of MLK3 by a Novel CEP1347-VHL-02 PROTAC Compound Limits the Oncogenic Potential of TNBC. Journal of medicinal chemistry, 67(17), 15012–15028. https://doi.org/10.1021/acs.jmedchem.4c00577
- Iwańska, O., Latoch, P., Kopik, N., Kovalenko, M., Lichocka, M., Serwa, R., & Starosta, A. L. (2024). Translation in Bacillus subtilis is spatially and temporally coordinated during sporulation. Nature communications, 15(1), 7188. https://doi.org/10.1038/s41467-024-51654-6
- Dubey, A. A., Sarkar, A., Milcz, K., Szulc, N. A., Thapa, P., Piechota, M., Serwa, R. A., & Pokrzywa, W. (2024). Floxuridine supports UPS independent of germline signaling and proteostasis regulators via involvement of detoxification in C. elegans. PLoS genetics, 20(7), e1011371. https://doi.org/10.1371/journal.pgen.1011371
- Warminski, M., Trepkowska, E., Smietanski, M., Sikorski, P. J., Baranowski, M. R., Bednarczyk, M., Kedzierska, H., Majewski, B., Mamot, A., Papiernik, D., Popielec, A., Serwa, R. A., Shimanski, B. A., Sklepkiewicz, P., Sklucka, M., Sokolowska, O., Spiewla, T., Toczydlowska-Socha, D., Warminska, Z., Wolosewicz, K., … Kowalska, J. (2024). Trinucleotide mRNA Cap Analogue N6-Benzylated at the Site of Posttranscriptional m6Am Mark Facilitates mRNA Purification and Confers Superior Translational Properties In Vitro and In Vivo. Journal of the American Chemical Society, 146(12), 8149–8163. https://doi.org/10.1021/jacs.3c12629
- Krakowczyk, M., Lenkiewicz, A. M., Sitarz, T., Malinska, D., Borrero, M., Mussulini, B. H. M., Linke, V., Szczepankiewicz, A. A., Biazik, J. M., Wydrych, A., Nieznanska, H., Serwa, R. A., Chacinska, A., & Bragoszewski, P. (2024). OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization. The Journal of cell biology, 223(5), e202306051. https://doi.org/10.1083/jcb.202306051
- Torres-Ayuso, P., Katerji, M., Mehlich, D., Lookingbill, S. A., Sabbasani, V. R., Liou, H., Casillas, A. L., Chauhan, S. S., Serwa, R., Rubin, M. R., Marusiak, A. A., Swenson, R. E., Warfel, N. A., & Brognard, J. (2024). PIM1 targeted degradation prevents the emergence of chemoresistance in prostate cancer. Cell chemical biology, 31(2), 326–337.e11. https://doi.org/10.1016/j.chembiol.2023.10.023
- Thapa, P., Olek, K., Kowalska, A., Serwa, R. A., & Pokrzywa, W. (2023). SAM, SAH and C. elegans longevity: insights from a partial AHCY deficiency model. npj aging, 9(1), 27. https://doi.org/10.1038/s41514-023-00125-1
- Kim, M., Serwa, R. A., Samluk, L., Suppanz, I., Kodroń, A., Stępkowski, T. M., Elancheliyan, P., Tsegaye, B., Oeljeklaus, S., Wasilewski, M., Warscheid, B., & Chacinska, A. (2023). Immunoproteasome-specific subunit PSMB9 induction is required to regulate cellular proteostasis upon mitochondrial dysfunction. Nature communications, 14(1), 4092. https://doi.org/10.1038/s41467-023-39642-8
- Wolczyk, M., Serwa, R., Kominek, A., Klejman, A., Milek, J., Chwałek, M., Turos-Korgul, L., Charzyńska, A., Dabrowski, M., Dziembowska, M., Skorski, T., Piwocka, K., & Podszywalow-Bartnicka, P. (2023). TIAR and FMRP shape pro-survival nascent proteome of leukemia cells in the bone marrow microenvironment. iScience, 26(4), 106543. https://doi.org/10.1016/j.isci.2023.106543
- Slusarczyk, P., Mandal, P. K., Zurawska, G., Niklewicz, M., Chouhan, K., Mahadeva, R., Jończy, A., Macias, M., Szybinska, A., Cybulska-Lubak, M., Krawczyk, O., Herman, S., Mikula, M., Serwa, R., Lenartowicz, M., Pokrzywa, W., & Mleczko-Sanecka, K. (2023). Impaired iron recycling from erythrocytes is an early hallmark of aging. eLife, 12, e79196. https://doi.org/10.7554/eLife.79196
- Chojnacka, K. J., Elancheliyan, P., Mussulini, B. H. M., Mohanraj, K., Callegari, S., Gosk, A., Banach, T., Góral, T., Szczepanowska, K., Rehling, P., Serwa, R. A., & Chacinska, A. (2022). Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III-specific assembly factor in mitochondria. Molecular biology of the cell, 33(4), ar29. https://doi.org/10.1091/mbc.E21-03-0143
- Małolepsza, J., Marchwicka, A., Serwa, R. A., Niinivehmas, S. P., Pentikäinen, O. T., Gendaszewska-Darmach, E., & Błażewska, K. M. (2022). Rational design, optimization, and biological evaluation of novel α-Phosphonopropionic acids as covalent inhibitors of Rab geranylgeranyl transferase. Journal of Enzyme Inhibition and Medicinal Chemistry, 37(1), 940–951. https://doi.org/10.1080/14756366.2022.2053525
- Sladowska, M., Turek, M., Kim, M.-J., Drabikowski, K., Mussulini, B. H. M., Mohanraj, K., Serwa, R. A., Topf, U., & Chacinska, A. (2021). Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans. PLOS Biology, 19(7), e3001302. https://doi.org/10.1371/journal.pbio.3001302
Equipment
All the measurements performed at the PCF IMol PAS are made using a Dionex UltiMate 3000 nano-LC system (equipped with a fraction collector) coupled to a Q-Exactive HF-X via an EASY-Spray ion source (all Thermo Fisher Scientific).
Q-Exactive HF-X is a high-performance hybrid quadrupole-orbitrap instrument characterised by superb sensitivity and scan speed. Dionex UltiMate 3000 nano-LC system equipped with a fraction collector allows automated 2D separation of peptides prior to their measurement on the Q-Exactive HF-X to provide increased depth and reproducibility of results. EASY-Spray ion source uses integrated, temperature-controlled column-emitter units to maximize nano-LC performance by generating narrow peaks, maximum separation efficiency and outstanding MS sensitivity.
This analytical platform is ideal for shotgun proteomics. Shotgun proteomics utilizes digestion of proteins into peptides which are then sequenced in the mass spectrometer and act as surrogates for the presence of proteins from which they are derived. Besides insights into protein expression levels and the extent of posttranslational modifications, this mode of analysis can be applied to provide information about protein turnover, subcellular localization, as well as protein-protein and protein-small molecule interactions.
Proteomics Core Facility
(PCF) IMol PAS Regulations
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These regulations provide a uniform guideline to the operations and services provided by the PCF IMol PAS to internal and external users.
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These regulations provide a guideline for soliciting services, ordering services, and paying for services provided by the PCF IMol PAS.
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Direct use of the equipment allocated at the PCF IMol PAS is restricted to the PCF IMol PAS Staff.
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The equipment allocated at the PCF IMol PAS may be used to provide services to internal and external users.
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Proposals of scientific collaborations between external users and heads of research groups at IMol PAS, requiring the use of the resources allocated at the PCF IMol PAS, need the approval of the committee consisting of the Director of IMol PAS, his or her deputies, and the head of the PCF IMol PAS.
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The list of prices for the services provided by the PCF IMol PAS is set by the Director’s Order.
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Users are obliged to familiarize themselves with regulations 1-22 and confirm this fact by clicking the accept icon on the online interest submission form.
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The services offered by the PCF IMol PAS will be adapted to the users’ needs. They scope of services includes:
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basic services (sample measurement, standard sample preparation: tryptic digest, peptide clean up),
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additional preparative services (e.g. isobaric TMT labelling of peptides, enrichment of phosphorylated/biotinylated/ubiquitinated/etc. peptides/proteins, peptide fractionation),
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consulting services (experimental design, customized sample preparation protocols, and post-experiment recommendations),
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data analytical services (results are returned to users as MaxQuant output tables free of charge, any further data analysis/mining will be considered additional service.
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Prices for the common services are listed on the PCF IMol PAS website (www.imol.institute/proteomics-core-facility) and users are free to inquire about the cost of less common services that have not been listed. The PCF IMol PAS Staff is responsible for scheduling the services. Generally, user requests are being processed on a first come, first served basis. In justified cases (e.g. optimization of instrument usage or to ensure the reproducibility of serial measurements) an exception can be made and a divergent scheduling order may be applied.
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The head of the PCF IMol PAS reserves the right to reject requests for the provision of services in objectively justified cases. In the event of a refusal, constructive feedback will be provided to the user.
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All users (internal or external) intending to submit samples for the measurement at the PCF IMol PAS are first requested to submit a brief proteomic experiment description via an online submission form.
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Proposals submitted via the online form will be evaluated and the information regarding the acceptance or rejection will be sent within 14 days by the PCF IMol PAS staff to the e-mail address provided in the form.
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In case of acceptance, the user will be invited to a remote meeting. During this meeting the most optimal analytical strategy is agreed as well as the involvement of PCF IMol PAS Staff and the estimated cost of services, calculated based on the Pricelist. A twenty-minute consultation per dataset is free. This time is sufficient to discuss most experiments. Consultations for more complex experiments, which may need beyond 20 min, will be considered as an additional service, charged based on the current price list.
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Before the samples are handed over, the user needs to agree to cover the cost of services by signing a purchase order form sent by the PCF IMol PAS Staff following the consultation. The form needs to be signed, scanned and emailed back to the address it was sent from.
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Users are required to follow sample preparation protocol approved by the PCF IMol PAS head. Any modification (e.g. resulted from a human error) should be reported before the samples are handed over for the measurement. Users who are discovered not to stick to this important rule, will be banned from submitting future samples.
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Users can request bespoke sample preparation training. The cost is estimated based on specific needs of the user.
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Upon completion of services users will be provided with results (in the form agreed during the remote meeting, see regulation 11). We aim to deliver the results within 21 days, counting from the day the samples are received by the PCF IMol PAS Staff.
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Within two weeks of the completion of services, users will be emailed (to the address provided in the online interest submission form) invoices. Upon request, original invoice documents will be sent by mail (Poczta Polska).
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The results, MaxQuant output tables (and raw files from the measurements, if requested) are being made available to the users in adequate form (e-mail, web-based file transfer, direct deposition on external hard drives, etc.).
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Raw data files from the measurements of external users’ samples will be stored by PCF IMol PAS for at least 3 months. If these raw data files are not requested by the user within this time, the PCF IMol PAS reserves the right to delete them.
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Acknowledgment: Any service provided by the PCF IMol PAS must be clearly indicated in the acknowledgments section of resulting publications. This is true even if relatively basic service is provided (standard sample preparation and/or standard measurement and/or standard data processing to produce MaxQuant output tables). Upon request, users will be provided with a generic statement about the instrumentation, data acquisition, and search parameters will be provided by the PCF IMol PAS Staff.
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Co-authorship: When a significant intellectual contribution from PCF Imol PAS Staff has been requested and delivered, their work must be acknowledged by naming them as co-authors of resulting publications. This is a default mode of agreement for experiments involving development or optimization of methods (in relation to sample preparation or data acquisition) or extensive data processing and/or mining. A selection of publication-ready figures and an input into writing of the relevant sections of the paper will be provided.
Price list
Service / net price PLN
Chemical Proteomics Platform Price List
PISA profiling* or chemical probe-based profiling** in cells – please inquire (exemplary quote for a set of 18 samples: 15,730 PLN total, i.e. < 875 PLN per sample)
*PISA profiling includes (cell preparation and treatment with bioactive compounds, protein sample preparation, protein concentration determination, tryptic digest, TMT-labelling of peptides, peptide fractionation, LC-MS/MS measurements (method 150 min) for 8 peptide fractions, data processing and storage. Frozen stocks of cells and bioactive compounds to be provided by the client.
** Chemical probe-based profiling includes (cell preparation and treatment with bioactive compounds and chemical probes, protein sample preparation, protein concentration determination, tryptic digest, probe-modified peptide enrichment, TMT-labelling of peptides, peptide fractionation, LC-MS/MS measurements (method 120 min) for 6 peptide fractions, data processing and storage. Frozen stocks of cells and bioactive compounds to be provided by the client.
Order form