Science & Insights
Welcome to our science section. Here, we present a curated selection of scientific publications, application notes, and other relevant research materials that highlight trenzyme’s ongoing commitment to innovation and scientific excellence.
Our contributions reflect our expertise in cell line development, recombinant protein production, and iPSC-based solutions, supporting scientists and partners worldwide in their research and development efforts.
This page will be continuously updated as we expand our portfolio of scientific insights and collaborative achievements. If you have any questions or would like to learn more about our scientific work, please feel free to ➥contact us.
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Application Notes
A High-Throughput Screening (HTS) Approach to Express the Difficult-To-Express Protein DEK in Human HEK293
trenzyme’s New Baculovirus-Free Expression System
Recombinant expression of 15N-labeled protein in E.coli by high cell density cultivation
Adaption of Cell Lines to Serum-Free Media
QC Portfolio of trenzyme to Ensure Pluripotency and Marker Expression of iPS Cell Line
Testing of hepatotoxic compounds for cytotoxicity and lipid accumulation
Relevant Publications Suitable to Our Services
This selection of publications highlights scientific studies in which trenzyme contributed as a service provider for protein expression and cell culture services. These collaborations demonstrate the quality and relevance of our work in supporting cutting-edge research.
2024
Tsaalbi-Shtylik, Anastasia; Mingard, Cécile; Räz, Michael; Oka, Rurika; Manders, Freek; Boxtel, Ruben Van; Wind, Niels De; Sturla, Shana J.
DNA mismatch repair controls the mutagenicity of Polymerase ζ-dependent translesion synthesis at methylated guanines Journal Article Protein Production Services
In: DNA Repair, vol. 142, 2024, ISSN: 1568-7864.
@article{Tsaalbi-Shtylik2024,
title = {DNA mismatch repair controls the mutagenicity of Polymerase ζ-dependent translesion synthesis at methylated guanines},
author = {Anastasia Tsaalbi-Shtylik and Cécile Mingard and Michael Räz and Rurika Oka and Freek Manders and Ruben Van Boxtel and Niels De Wind and Shana J. Sturla},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service},
doi = {10.1016/j.dnarep.2024.103755},
issn = {1568-7864},
year = {2024},
date = {2024-10-00},
urldate = {2024-10-00},
journal = {DNA Repair},
volume = {142},
publisher = {Elsevier BV},
abstract = {By replicating damaged nucleotides, error-prone DNA translesion synthesis (TLS) enables the completion of replication, albeit at the expense of fidelity. TLS of helix-distorting DNA lesions, that usually have reduced capacity of basepairing, comprises insertion opposite the lesion followed by extension, the latter in particular by polymerase ζ (Pol ζ). However, little is known about involvement of Pol ζ in TLS of non- or poorly-distorting, but miscoding, lesions such as O6-methyldeoxyguanosine (O6-medG). Using purified Pol ζ we describe that the enzyme can misincorporate thymidine opposite O6-medG and efficiently extend from terminal mismatches, suggesting its involvement in the mutagenicity of O6-medG. Surprisingly, O6-medG lesions induced by the methylating agent N-methyl-N’-nitro-N-nitrosoguanidine (MNNG) appeared more, rather than less, mutagenic in Pol ζ-deficient mouse embryonic fibroblasts (MEFs) than in wild type MEFs. This suggested that in vivo Pol ζ participates in non-mutagenic TLS of O6-medG. However, we found that the Pol ζ-dependent misinsertions at O6-medG lesions are efficiently corrected by DNA mismatch repair (MMR), which masks the error-proneness of Pol ζ. We also found that the MNNG-induced mutational signature is determined by the adduct spectrum, and modulated by MMR. The signature mimicked single base substitution signature 11 in the catalogue of somatic mutations in cancer, associated with treatment with the methylating drug temozolomide. Our results unravel the individual roles of the major contributors to methylating drug-induced mutagenesis. Moreover, these results warrant caution as to the classification of TLS as mutagenic or error-free based on in vitro data or on the analysis of mutations induced in MMR-proficient cells.},
keywords = {TLS},
pubstate = {published},
tppubtype = {article}
}
By replicating damaged nucleotides, error-prone DNA translesion synthesis (TLS) enables the completion of replication, albeit at the expense of fidelity. TLS of helix-distorting DNA lesions, that usually have reduced capacity of basepairing, comprises insertion opposite the lesion followed by extension, the latter in particular by polymerase ζ (Pol ζ). However, little is known about involvement of Pol ζ in TLS of non- or poorly-distorting, but miscoding, lesions such as O6-methyldeoxyguanosine (O6-medG). Using purified Pol ζ we describe that the enzyme can misincorporate thymidine opposite O6-medG and efficiently extend from terminal mismatches, suggesting its involvement in the mutagenicity of O6-medG. Surprisingly, O6-medG lesions induced by the methylating agent N-methyl-N’-nitro-N-nitrosoguanidine (MNNG) appeared more, rather than less, mutagenic in Pol ζ-deficient mouse embryonic fibroblasts (MEFs) than in wild type MEFs. This suggested that in vivo Pol ζ participates in non-mutagenic TLS of O6-medG. However, we found that the Pol ζ-dependent misinsertions at O6-medG lesions are efficiently corrected by DNA mismatch repair (MMR), which masks the error-proneness of Pol ζ. We also found that the MNNG-induced mutational signature is determined by the adduct spectrum, and modulated by MMR. The signature mimicked single base substitution signature 11 in the catalogue of somatic mutations in cancer, associated with treatment with the methylating drug temozolomide. Our results unravel the individual roles of the major contributors to methylating drug-induced mutagenesis. Moreover, these results warrant caution as to the classification of TLS as mutagenic or error-free based on in vitro data or on the analysis of mutations induced in MMR-proficient cells.
Auclair, Guy; Muñoz-Piñeiro, Amalia; Charoud-Got, Jean; Paleari, Renata; Kaiser, Patricia; Arsene, Cristian-Gabriel; Trapmann, Stefanie; Mosca, Andrea; Deprez, Liesbet
Certification of the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin in blood haemolysate: ERM®-DA485/IFCC and ERM®-DA486/IFCC Journal Article Protein Production Services
In: ERM®-DA485/IFCC and ERM®-DA486/IFCC, Publications Office of the European Union, 2024, 2024, ISBN: 978-92-68-14954-6.
Abstract | Links | Tags: HbA2, P2020-193
@article{nokey,
title = {Certification of the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin in blood haemolysate: ERM®-DA485/IFCC and ERM®-DA486/IFCC},
author = {Guy Auclair and Amalia Muñoz-Piñeiro and Jean Charoud-Got and Renata Paleari and Patricia Kaiser and Cristian-Gabriel Arsene and Stefanie Trapmann and Andrea Mosca and Liesbet Deprez},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service
https://shop.trenzyme.com/products/hemoglobin-hba2-%CE%B12%CE%B42, ➥Mentioned protein in trenzyme webshop (SKU P2020-193)
},
doi = {10.2760/877530},
isbn = {978-92-68-14954-6},
year = {2024},
date = {2024-09-06},
urldate = {2024-09-06},
journal = {ERM®-DA485/IFCC and ERM®-DA486/IFCC, Publications Office of the European Union, 2024},
abstract = {ERM®-DA485/IFCC and ERM®-DA486/IFCC are blood haemolysate materials certified for the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin, produced within the scope of ISO 17034 accreditation [1]. The CRMs are available in glass vials containing at least 2 mL of blood haemolysate, lyophilised into a dry powder. The vials were sealed under an atmosphere of nitrogen. Between-unit homogeneity was quantified and stability during transport and storage was assessed in accordance with ISO 33405:2024 [2]. The minimum volume of reconstituted material to be used for one measurement is 5 μL. This minimum sampling volume gave acceptable repeatability using this sample volume, the within-unit inhomogeneity did not contribute to variation of measurement. The materials were characterised by a reference method [3] through an interlaboratory comparison of laboratories of demonstrated competence and adhering to ISO/IEC 17025:2017 [4]. All data sets obtained were found technically valid. Uncertainties of the certified values were calculated in accordance with ISO 17034:2016 [1] and include uncertainties related to possible inhomogeneity, instability and characterisation. The materials are intended for the calibration of various analytical methods used for the quantification of the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin in human blood. Before release of the CRMs, the certification project was subjected to peer-review involving both internal and external experts.},
keywords = {HbA2, P2020-193},
pubstate = {published},
tppubtype = {article}
}
ERM®-DA485/IFCC and ERM®-DA486/IFCC are blood haemolysate materials certified for the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin, produced within the scope of ISO 17034 accreditation [1]. The CRMs are available in glass vials containing at least 2 mL of blood haemolysate, lyophilised into a dry powder. The vials were sealed under an atmosphere of nitrogen. Between-unit homogeneity was quantified and stability during transport and storage was assessed in accordance with ISO 33405:2024 [2]. The minimum volume of reconstituted material to be used for one measurement is 5 μL. This minimum sampling volume gave acceptable repeatability using this sample volume, the within-unit inhomogeneity did not contribute to variation of measurement. The materials were characterised by a reference method [3] through an interlaboratory comparison of laboratories of demonstrated competence and adhering to ISO/IEC 17025:2017 [4]. All data sets obtained were found technically valid. Uncertainties of the certified values were calculated in accordance with ISO 17034:2016 [1] and include uncertainties related to possible inhomogeneity, instability and characterisation. The materials are intended for the calibration of various analytical methods used for the quantification of the amount-of-substance fraction of haemoglobin A2 versus total haemoglobin in human blood. Before release of the CRMs, the certification project was subjected to peer-review involving both internal and external experts.
Groetzner, Sarah
Miniaturized Drug Discovery Assays Targeting Macrophages in Fibrotic Diseases PhD Thesis Stem Cell ServicesGene Synthesis and Custom Cloning
2024.
@phdthesis{Groetzner2024Minia-70032,
title = {Miniaturized Drug Discovery Assays Targeting Macrophages in Fibrotic Diseases },
author = {Sarah Groetzner},
url = {https://kops.uni-konstanz.de/entities/publication/4ab6c1cf-1329-43f0-a99e-f7c1c42ebc76, ➥University Konstanz
https://kops.uni-konstanz.de/bitstreams/1467a309-38e1-4f8f-bce1-d76e2269e78d/download, ➥Publication Download
https://trenzyme.com/cell-culture-services/stem-cell-differentiation-service/, ➥Stem Cell Differentiation Service},
year = {2024},
date = {2024-04-16},
urldate = {2024-04-16},
abstract = {Macrophages have key regulatory functions in health and disease, such as fibrosis, and are therefore of high interest for drug discovery. Fibrosis is a result of chronic tissue damage leading to a deregulated wound healing process. Macrophages are involved in different phases of the fibrotic cascade and its onset is assumed to present a reaction to aberrant macrophage activation. Hence, there exists potential of modulating these cells for therapeutic benefits. In patients suffering from idiopathic pulmonary fibrosis (IPF), defective removal of apoptotic cells (efferocytosis) by macrophages was reported. Therefore, targeting macrophages and especially the modulation of their efferocytotic activity represents one strategy to diminish fibrotic processes in IPF. However, an impediment in drug discovery is the lack of physiologically relevant cellular in vitro models that can recapitulate the disease situation in patients. Most of the reported models lack relevant cells in sufficient quantity and thus, cannot be applied for screening campaigns. Hence, the aim of the presented work was to fill the gap of the unmet need for physiologically relevant in vitro drug discovery assays to target macrophage functions in fibrotic diseases. To access large numbers of model cells, an upscaled protocol was established for differentiation of human induced pluripotent stem cells (iPSCs) into progenitor cells and subsequent maturation into functional macrophages. These iPSC-derived macrophages (IDMs) resembled monocyte-derived macrophages (MDMs) both with respect to phenotypical and functional characteristics. To analyze macrophage functions in fibrotic diseases, a miniaturized high-content-imagingbased assay was established, enabling the analysis and quantification of both efferocytosis and phagocytosis for medium- to high-throughput applications. Utilizing IDMs and MDMs, the cells showed comparable pharmacology, as demonstrated by the analysis of Spleen tyrosine kinase (Syk) inhibitors, Dexamethasone, and a pro-fibrotic cocktail. Besides reduced efferocytotic function of macrophages, an accumulation of senescent cells is reported for IPF patients. To analyze the potential link between these two conditions, a miniaturized co-culture set-up was established. Using differently induced senescent epithelial cells, the inhibitory effect of senescence signals on efferocytosis and phagocytosis was shown in this context. On the contrary, senolytic treatment of senescent epithelial cells triggered their apoptosis induction and resulted in increased efferocytotic activity. The insights gained from this study imply that senescent cells may be a potential cause of reduced efferocytotic activity. Hence, addressing senescent cells and their communication with macrophages could present a promising therapeutical approach. 3 In conclusion, the here established iPSC-derived macrophage model in combination with the miniaturized efferocytosis and phagocytosis assays can be implemented into large-scale screening campaigns and may open new routes to innovative therapeutic paths in the context of fibrosis and beyond. },
keywords = {iPSC},
pubstate = {published},
tppubtype = {phdthesis}
}
Macrophages have key regulatory functions in health and disease, such as fibrosis, and are therefore of high interest for drug discovery. Fibrosis is a result of chronic tissue damage leading to a deregulated wound healing process. Macrophages are involved in different phases of the fibrotic cascade and its onset is assumed to present a reaction to aberrant macrophage activation. Hence, there exists potential of modulating these cells for therapeutic benefits. In patients suffering from idiopathic pulmonary fibrosis (IPF), defective removal of apoptotic cells (efferocytosis) by macrophages was reported. Therefore, targeting macrophages and especially the modulation of their efferocytotic activity represents one strategy to diminish fibrotic processes in IPF. However, an impediment in drug discovery is the lack of physiologically relevant cellular in vitro models that can recapitulate the disease situation in patients. Most of the reported models lack relevant cells in sufficient quantity and thus, cannot be applied for screening campaigns. Hence, the aim of the presented work was to fill the gap of the unmet need for physiologically relevant in vitro drug discovery assays to target macrophage functions in fibrotic diseases. To access large numbers of model cells, an upscaled protocol was established for differentiation of human induced pluripotent stem cells (iPSCs) into progenitor cells and subsequent maturation into functional macrophages. These iPSC-derived macrophages (IDMs) resembled monocyte-derived macrophages (MDMs) both with respect to phenotypical and functional characteristics. To analyze macrophage functions in fibrotic diseases, a miniaturized high-content-imagingbased assay was established, enabling the analysis and quantification of both efferocytosis and phagocytosis for medium- to high-throughput applications. Utilizing IDMs and MDMs, the cells showed comparable pharmacology, as demonstrated by the analysis of Spleen tyrosine kinase (Syk) inhibitors, Dexamethasone, and a pro-fibrotic cocktail. Besides reduced efferocytotic function of macrophages, an accumulation of senescent cells is reported for IPF patients. To analyze the potential link between these two conditions, a miniaturized co-culture set-up was established. Using differently induced senescent epithelial cells, the inhibitory effect of senescence signals on efferocytosis and phagocytosis was shown in this context. On the contrary, senolytic treatment of senescent epithelial cells triggered their apoptosis induction and resulted in increased efferocytotic activity. The insights gained from this study imply that senescent cells may be a potential cause of reduced efferocytotic activity. Hence, addressing senescent cells and their communication with macrophages could present a promising therapeutical approach. 3 In conclusion, the here established iPSC-derived macrophage model in combination with the miniaturized efferocytosis and phagocytosis assays can be implemented into large-scale screening campaigns and may open new routes to innovative therapeutic paths in the context of fibrosis and beyond.
Diofano, Federica; Amadi, Chidinma; Gahr, Bernd; Weinmann, Karolina; Rottbauer, Wolfgang; Just, Steffen
SMYD1-mediated Mono-Methylation of Lysine K35 of the sarcomeric Myosin Heavy Chain (MHC) is fundamental for thick filament assembly in zebrafish and human iPSC-derived cardiomyocytes Journal Article Protein Production Services
In: bioRxiv 2024.03.27.585692, 2024.
Abstract | Links | Tags: SMYD1
@article{Diofano2024,
title = {SMYD1-mediated Mono-Methylation of Lysine K35 of the sarcomeric Myosin Heavy Chain (MHC) is fundamental for thick filament assembly in zebrafish and human iPSC-derived cardiomyocytes},
author = {Federica Diofano and Chidinma Amadi and Bernd Gahr and Karolina Weinmann and Wolfgang Rottbauer and Steffen Just},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service},
doi = {10.1101/2024.03.27.585692},
year = {2024},
date = {2024-03-28},
urldate = {2024-03-28},
journal = {bioRxiv 2024.03.27.585692},
publisher = {Cold Spring Harbor Laboratory},
abstract = {The SMYD family is a unique class of lysine methyltransferases (KMTases) known to methylate histones but also non-histone proteins. Among the five SMYD family members (1-5), SMYD1 was identified as a heart- and skeletal muscle-specific KMTase, which, together with Unc45b and Hsp90a, interacts with Myosin thereby regulating thick filament assembly. However, the process by which SMYD1 orchestrates Myosin assembly is largely unknown. Here, we found that SMYD1 physically interacts with Myosin heavy chain (Myh) at its N-terminus and that the Myh N-terminus specifically gets mono-methylated by SMYD1 at lysine 35 (K35). Accordingly, methylated Myh is properly integrated into functional sarcomeres, whereas unmethylated Myh molecules in Smyd1-deficient zebrafish are efficiently degraded by the Ubiquitin Proteasome System (UPS) leading to defective thick filament assembly. Although the inhibition of the UPS by MG132 is able to reconstitute Myosin levels in Smyd1-deficient zebrafish embryos, thick filament assembly is still blocked due to the lack of K35 Myh mono-methylation. Similar to the situation in zebrafish striated muscle cells, SMYD1-mediated MYH methylation is also critical for thick filament assembly in human cardiomyocytes, indicating cross-species conservation of this fundamental mechanism of Myosin methylation, which has been first described about 40 years ago. Further investigations will now be essential to explore the therapeutic potential of targeting this pathway in cardiomyopathies and skeletal muscle disorders.},
howpublished = {bioRxiv},
keywords = {SMYD1},
pubstate = {published},
tppubtype = {article}
}
The SMYD family is a unique class of lysine methyltransferases (KMTases) known to methylate histones but also non-histone proteins. Among the five SMYD family members (1-5), SMYD1 was identified as a heart- and skeletal muscle-specific KMTase, which, together with Unc45b and Hsp90a, interacts with Myosin thereby regulating thick filament assembly. However, the process by which SMYD1 orchestrates Myosin assembly is largely unknown. Here, we found that SMYD1 physically interacts with Myosin heavy chain (Myh) at its N-terminus and that the Myh N-terminus specifically gets mono-methylated by SMYD1 at lysine 35 (K35). Accordingly, methylated Myh is properly integrated into functional sarcomeres, whereas unmethylated Myh molecules in Smyd1-deficient zebrafish are efficiently degraded by the Ubiquitin Proteasome System (UPS) leading to defective thick filament assembly. Although the inhibition of the UPS by MG132 is able to reconstitute Myosin levels in Smyd1-deficient zebrafish embryos, thick filament assembly is still blocked due to the lack of K35 Myh mono-methylation. Similar to the situation in zebrafish striated muscle cells, SMYD1-mediated MYH methylation is also critical for thick filament assembly in human cardiomyocytes, indicating cross-species conservation of this fundamental mechanism of Myosin methylation, which has been first described about 40 years ago. Further investigations will now be essential to explore the therapeutic potential of targeting this pathway in cardiomyopathies and skeletal muscle disorders.
Grzesiak, Jonas; Walter, Arne; Fellner, Lea; Brosig, Alexander; Horlacher, Reinhold; Möller, Ralf; Duschek, Frank
A mid-IR spectroscopic setup for identifying viruses in human saliva under high throughput conditions Conference Protein Production Services
VII. International Congress on Biophotonics, 2024.
Abstract | Links | Tags: P2020-001, P2020-016, P2020-025, SARS-CoV-2
@conference{dlr207356,
title = {A mid-IR spectroscopic setup for identifying viruses in human saliva under high throughput conditions},
author = {Jonas Grzesiak and Arne Walter and Lea Fellner and Alexander Brosig and Reinhold Horlacher and Ralf Möller and Frank Duschek},
url = {https://elib.dlr.de/207356/, ➥Publication Link
https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service
https://trenzyme.shop/products/spike-s1-rbd-liquid, ➥Mentioned protein in trenzyme webshop (SKU P2020-001)
https://shop.trenzyme.com/products/hace2-protein-ecd, ➥Mentioned protein in trenzyme webshop (SKU P2020-016)
https://shop.trenzyme.com/products/s-protein-stabilized-trimer, ➥Mentioned protein in trenzyme webshop (SKU P2020-025)},
year = {2024},
date = {2024-03-03},
urldate = {2024-03-03},
booktitle = {VII. International Congress on Biophotonics},
abstract = {Mid-IR-Spectroscopy promises high selective capabilities for the detection of viruses such as SARS-CoV2 in human saliva. The motivation for this work was driven by the demand for enhanced COVID testing capabilities, especially in scenarios with large number of people passing, e.g. at airports. To achieve this, high and fast throughput of taken saliva samples is required. Additionally, high true positive rates are essential, when identifying the viral signatures e.g. by machine learning techniques. In this progress report, we present our approach for a high and fast throughput detection setup: The mid-IR spectroscopy part is based on quantum cascade lasers (QCL) and attenuated total reflection flow cells. To enrich the concentration of the viral load in the saliva sample, we use ctionalized magnetic beads. The sample handling part is designed to be automatized for the later application. This can allow for a much faster spectral scan than compared to for example FTIR methods and a possible higher throughput of samples, as for example for Raman microscopy approaches. In our setting, detecting low concentrations of viral loads in aqueous solutions is challenging due to the dynamic range required for the detectors. We present a balanced detection approach to achieve a reasonable dynamic range and discuss the implications for the
automatized identification. The diversion of sample material during the cleaning procedure of the flow cells, the purification process with the protein-coated magnetic beads and other impurities can cause variations in the amide I and amide II vibration bands, disturbing the virus signatures. Along our measured spectra we discuss these upcoming challenges for the AI-based reliable identification of the viruses with respect to the creation of training datasets.},
keywords = {P2020-001, P2020-016, P2020-025, SARS-CoV-2},
pubstate = {published},
tppubtype = {conference}
}
Mid-IR-Spectroscopy promises high selective capabilities for the detection of viruses such as SARS-CoV2 in human saliva. The motivation for this work was driven by the demand for enhanced COVID testing capabilities, especially in scenarios with large number of people passing, e.g. at airports. To achieve this, high and fast throughput of taken saliva samples is required. Additionally, high true positive rates are essential, when identifying the viral signatures e.g. by machine learning techniques. In this progress report, we present our approach for a high and fast throughput detection setup: The mid-IR spectroscopy part is based on quantum cascade lasers (QCL) and attenuated total reflection flow cells. To enrich the concentration of the viral load in the saliva sample, we use ctionalized magnetic beads. The sample handling part is designed to be automatized for the later application. This can allow for a much faster spectral scan than compared to for example FTIR methods and a possible higher throughput of samples, as for example for Raman microscopy approaches. In our setting, detecting low concentrations of viral loads in aqueous solutions is challenging due to the dynamic range required for the detectors. We present a balanced detection approach to achieve a reasonable dynamic range and discuss the implications for the
automatized identification. The diversion of sample material during the cleaning procedure of the flow cells, the purification process with the protein-coated magnetic beads and other impurities can cause variations in the amide I and amide II vibration bands, disturbing the virus signatures. Along our measured spectra we discuss these upcoming challenges for the AI-based reliable identification of the viruses with respect to the creation of training datasets.
automatized identification. The diversion of sample material during the cleaning procedure of the flow cells, the purification process with the protein-coated magnetic beads and other impurities can cause variations in the amide I and amide II vibration bands, disturbing the virus signatures. Along our measured spectra we discuss these upcoming challenges for the AI-based reliable identification of the viruses with respect to the creation of training datasets.
Scientific Posters
Modular System for Efficient Screening and Optimized Production of Difficult-To-Express Target Proteins
Festival of Biologics 2025 in Basel:
Flexible System for Faster Screening and High-Yield Production of Complex Target Proteins
2024:
