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
Diofano, Federica; Amadi, Chidinma; Gahr, Bernd; Weinmann, Karolina; Rottbauer, Wolfgang; Just, Steffen
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
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.
Reis-Claro, Inês; Silva, Maria Inês; Moutinho, Ana; Garcia, Beatriz C.; Pereira-Castro, Isabel; Moreira, Alexandra
Application of the iPLUS non-coding sequence in improving biopharmaceuticals production Journal Article
In: Front. Bioeng. Biotechnol., vol. 12, 2024, ISSN: 2296-4185.
Abstract | Links | Tags: iPLUS, pTZ-p04_GFP
@article{Reis-Claro2024,
title = {Application of the iPLUS non-coding sequence in improving biopharmaceuticals production},
author = {Inês Reis-Claro and Maria Inês Silva and Ana Moutinho and Beatriz C. Garcia and Isabel Pereira-Castro and Alexandra Moreira},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service},
doi = {10.3389/fbioe.2024.1355957},
issn = {2296-4185},
year = {2024},
date = {2024-02-06},
urldate = {2024-02-06},
journal = {Front. Bioeng. Biotechnol.},
volume = {12},
publisher = {Frontiers Media SA},
abstract = {The biotechnological landscape has witnessed significant growth in biological therapeutics particularly in the field of recombinant protein production. Here we investigate the function of 3′UTR cis-regulatory elements in increasing mRNA and protein levels in different biological therapeutics and model systems, spanning from monoclonal antibodies to mRNA vaccines. We explore the regulatory function of iPLUS - a universal sequence capable of consistently augmenting recombinant protein levels. By incorporating iPLUS in a vector to express a monoclonal antibody used in immunotherapy, in a mammalian cell line used by the industry (ExpiCHO), trastuzumab production increases by 2-fold. As yeast Pichia pastoris is widely used in the manufacture of industrial enzymes and pharmaceuticals, we then used iPLUS in tandem (3x) and iPLUSv2 (a variant of iPLUS) to provide proof-of-concept data that it increases the production of a reporter protein more than 100-fold. As iPLUS functions by also increasing mRNA levels, we hypothesize that these sequences could be used as an asset in the mRNA vaccine industry. In fact, by including iPLUSv2 downstream of Spike we were able to double its production. Moreover, the same effect was observed when we introduced iPLUSv2 downstream of MAGEC2, a tumor-specific antigen tested for cancer mRNA vaccines. Taken together, our study provides data (TLR4) showing that iPLUS may be used as a valuable asset in a variety of systems used by the biotech and biopharmaceutical industry. Our results underscore the critical role of non-coding sequences in controlling gene expression, offering a promising avenue to accelerate, enhance, and cost-effectively optimize biopharmaceutical production processes.},
keywords = {iPLUS, pTZ-p04_GFP},
pubstate = {published},
tppubtype = {article}
}
The biotechnological landscape has witnessed significant growth in biological therapeutics particularly in the field of recombinant protein production. Here we investigate the function of 3′UTR cis-regulatory elements in increasing mRNA and protein levels in different biological therapeutics and model systems, spanning from monoclonal antibodies to mRNA vaccines. We explore the regulatory function of iPLUS - a universal sequence capable of consistently augmenting recombinant protein levels. By incorporating iPLUS in a vector to express a monoclonal antibody used in immunotherapy, in a mammalian cell line used by the industry (ExpiCHO), trastuzumab production increases by 2-fold. As yeast Pichia pastoris is widely used in the manufacture of industrial enzymes and pharmaceuticals, we then used iPLUS in tandem (3x) and iPLUSv2 (a variant of iPLUS) to provide proof-of-concept data that it increases the production of a reporter protein more than 100-fold. As iPLUS functions by also increasing mRNA levels, we hypothesize that these sequences could be used as an asset in the mRNA vaccine industry. In fact, by including iPLUSv2 downstream of Spike we were able to double its production. Moreover, the same effect was observed when we introduced iPLUSv2 downstream of MAGEC2, a tumor-specific antigen tested for cancer mRNA vaccines. Taken together, our study provides data (TLR4) showing that iPLUS may be used as a valuable asset in a variety of systems used by the biotech and biopharmaceutical industry. Our results underscore the critical role of non-coding sequences in controlling gene expression, offering a promising avenue to accelerate, enhance, and cost-effectively optimize biopharmaceutical production processes.
Behrsing, Thomas; Blair, Victoria L.; Jaroschik, Florian; Deacon, Glen B.; Junk, Peter C.
Rare Earths—The Answer to Everything Journal Article
In: Molecules, vol. 29, no. 3, 2024, ISSN: 1420-3049.
Abstract | Links | Tags: LanM, P2020-126
@article{Behrsing2024,
title = {Rare Earths—The Answer to Everything},
author = {Thomas Behrsing and Victoria L. Blair and Florian Jaroschik and Glen B. Deacon and Peter C. Junk},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service
https://shop.trenzyme.com/products/lanm, ➥Mentioned protein in trenzyme webshop (SKU P2020-126)},
doi = {10.3390/molecules29030688},
issn = {1420-3049},
year = {2024},
date = {2024-02-01},
urldate = {2024-02-01},
journal = {Molecules},
volume = {29},
number = {3},
publisher = {MDPI AG},
abstract = {Rare earths, scandium, yttrium, and the fifteen lanthanoids from lanthanum to lutetium, are classified as critical metals because of their ubiquity in daily life. They are present in magnets in cars, especially electric cars; green electricity generating systems and computers; in steel manufacturing; in glass and light emission materials especially for safety lighting and lasers; in exhaust emission catalysts and supports; catalysts in artificial rubber production; in agriculture and animal husbandry; in health and especially cancer diagnosis and treatment; and in a variety of materials and electronic products essential to modern living. They have the potential to replace toxic chromates for corrosion inhibition, in magnetic refrigeration, a variety of new materials, and their role in agriculture may expand. This review examines their role in sustainability, the environment, recycling, corrosion inhibition, crop production, animal feedstocks, catalysis, health, and materials, as well as considering future uses.},
keywords = {LanM, P2020-126},
pubstate = {published},
tppubtype = {article}
}
Rare earths, scandium, yttrium, and the fifteen lanthanoids from lanthanum to lutetium, are classified as critical metals because of their ubiquity in daily life. They are present in magnets in cars, especially electric cars; green electricity generating systems and computers; in steel manufacturing; in glass and light emission materials especially for safety lighting and lasers; in exhaust emission catalysts and supports; catalysts in artificial rubber production; in agriculture and animal husbandry; in health and especially cancer diagnosis and treatment; and in a variety of materials and electronic products essential to modern living. They have the potential to replace toxic chromates for corrosion inhibition, in magnetic refrigeration, a variety of new materials, and their role in agriculture may expand. This review examines their role in sustainability, the environment, recycling, corrosion inhibition, crop production, animal feedstocks, catalysis, health, and materials, as well as considering future uses.
Odak, Ivan; Riemann, Lennart; Sandrock, Inga; Cossmann, Anne; Ramos, Gema Morillas; Hammerschmidt, Swantje I.; Ritter, Christiane; Friedrichsen, Michaela; Hassan, Ahmed; Dopfer-Jablonka, Alexandra; Stankov, Metodi V.; Weskamm, Leonie M.; Addo, Marylyn M.; Ravens, Inga; Willenzon, Stefanie; Schimrock, Anja; Ristenpart, Jasmin; Janssen, Anika; Barros-Martins, Joana; Hansen, Gesine; Falk, Christine; Behrens, Georg M. N.; Förster, Reinhold
Systems biology analysis reveals distinct molecular signatures associated with immune responsiveness to the BNT162b COVID-19 vaccine Journal Article
In: eBioMedicine, vol. 99, 2024, ISSN: 2352-3964.
Abstract | Links | Tags: P2020-001, SARS-CoV-2
@article{Odak2024,
title = {Systems biology analysis reveals distinct molecular signatures associated with immune responsiveness to the BNT162b COVID-19 vaccine},
author = {Ivan Odak and Lennart Riemann and Inga Sandrock and Anne Cossmann and Gema Morillas Ramos and Swantje I. Hammerschmidt and Christiane Ritter and Michaela Friedrichsen and Ahmed Hassan and Alexandra Dopfer-Jablonka and Metodi V. Stankov and Leonie M. Weskamm and Marylyn M. Addo and Inga Ravens and Stefanie Willenzon and Anja Schimrock and Jasmin Ristenpart and Anika Janssen and Joana Barros-Martins and Gesine Hansen and Christine Falk and Georg M.N. Behrens and Reinhold Förster},
url = {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)},
doi = {10.1016/j.ebiom.2023.104947},
issn = {2352-3964},
year = {2024},
date = {2024-01-00},
urldate = {2024-01-00},
journal = {eBioMedicine},
volume = {99},
publisher = {Elsevier BV},
abstract = {Background
Human immune responses to COVID-19 vaccines display a large heterogeneity of induced immunity and the underlying immune mechanisms for this remain largely unknown.
Methods
Using a systems biology approach, we longitudinally profiled a unique cohort of female high and low responders to the BNT162b vaccine, who were known from previous COVID-19 vaccinations to develop maximum and minimum immune responses to the vaccine. We utilized high dimensional flow cytometry, bulk and single cell mRNA sequencing and 48-plex serum cytokine analyses.
Findings
We revealed early, transient immunological and molecular signatures that distinguished high from low responders and correlated with B and T cell responses measured 14 days later. High responders featured a distinct transcriptional activity of interferon-driven genes and genes connected to enhanced antigen presentation. This was accompanied by a robust cytokine response related to Th1 differentiation. Both transcriptome and serum cytokine signatures were confirmed in two independent confirmatory cohorts.
Interpretation
Collectively, our data contribute to a better understanding of the immunogenicity of mRNA-based COVID-19 vaccines, which might lead to the optimization of vaccine designs for individuals with poor vaccine responses.
Funding
German Center for Infection Research, German Center for Lung Research, German Research Foundation, Excellence Strategy EXC 2155 “RESIST” and European Regional Development Fund.},
keywords = {P2020-001, SARS-CoV-2},
pubstate = {published},
tppubtype = {article}
}
Background
Human immune responses to COVID-19 vaccines display a large heterogeneity of induced immunity and the underlying immune mechanisms for this remain largely unknown.
Methods
Using a systems biology approach, we longitudinally profiled a unique cohort of female high and low responders to the BNT162b vaccine, who were known from previous COVID-19 vaccinations to develop maximum and minimum immune responses to the vaccine. We utilized high dimensional flow cytometry, bulk and single cell mRNA sequencing and 48-plex serum cytokine analyses.
Findings
We revealed early, transient immunological and molecular signatures that distinguished high from low responders and correlated with B and T cell responses measured 14 days later. High responders featured a distinct transcriptional activity of interferon-driven genes and genes connected to enhanced antigen presentation. This was accompanied by a robust cytokine response related to Th1 differentiation. Both transcriptome and serum cytokine signatures were confirmed in two independent confirmatory cohorts.
Interpretation
Collectively, our data contribute to a better understanding of the immunogenicity of mRNA-based COVID-19 vaccines, which might lead to the optimization of vaccine designs for individuals with poor vaccine responses.
Funding
German Center for Infection Research, German Center for Lung Research, German Research Foundation, Excellence Strategy EXC 2155 “RESIST” and European Regional Development Fund.
Human immune responses to COVID-19 vaccines display a large heterogeneity of induced immunity and the underlying immune mechanisms for this remain largely unknown.
Methods
Using a systems biology approach, we longitudinally profiled a unique cohort of female high and low responders to the BNT162b vaccine, who were known from previous COVID-19 vaccinations to develop maximum and minimum immune responses to the vaccine. We utilized high dimensional flow cytometry, bulk and single cell mRNA sequencing and 48-plex serum cytokine analyses.
Findings
We revealed early, transient immunological and molecular signatures that distinguished high from low responders and correlated with B and T cell responses measured 14 days later. High responders featured a distinct transcriptional activity of interferon-driven genes and genes connected to enhanced antigen presentation. This was accompanied by a robust cytokine response related to Th1 differentiation. Both transcriptome and serum cytokine signatures were confirmed in two independent confirmatory cohorts.
Interpretation
Collectively, our data contribute to a better understanding of the immunogenicity of mRNA-based COVID-19 vaccines, which might lead to the optimization of vaccine designs for individuals with poor vaccine responses.
Funding
German Center for Infection Research, German Center for Lung Research, German Research Foundation, Excellence Strategy EXC 2155 “RESIST” and European Regional Development Fund.
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:
