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.
2026
Horvath, Dennis; Inholz, Katharina; Mink, Dennis; Madel, Alicia; Koerner, Julia; Horlacher, Reinhold; Basler, Michael
PLGA‐particle‐based vaccine induces SARS‐CoV‐2‐specific antibody and T‐cell responses Journal Article
In: British J Pharmacology, 2026, ISSN: 1476-5381.
Abstract | Links | Tags: SARS-CoV-2
@article{Horvath2026,
title = {PLGA‐particle‐based vaccine induces SARS‐CoV‐2‐specific antibody and T‐cell responses},
author = {Dennis Horvath and Katharina Inholz and Dennis Mink and Alicia Madel and Julia Koerner and Reinhold Horlacher and Michael Basler},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service},
doi = {10.1111/bph.70423},
issn = {1476-5381},
year = {2026},
date = {2026-04-01},
urldate = {2026-04-01},
journal = {British J Pharmacology},
publisher = {Wiley},
abstract = {Background and Purpose
Current coronavirus disease 2019 (COVID-19) vaccines effectively prevent severe disease but induce primarily systemic immunity without mucosal protection in the respiratory tract, which is mandatory for protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection and the prevention of viral transmission. Vaccination strategies capable of inducing local immunity at the site of infection are therefore needed. Here, we evaluated a poly (lactic-co-glycolic acid) (PLGA) microparticle-based vaccine co-encapsulating the receptor binding domain (RBD) of SARS-CoV-2 Spike protein with the TLR3/RIG-1 agonist Riboxxim, employing a subcutaneous prime and intranasal boost immunization schedule.
Experimental Approach
BALB/c mice received subcutaneous prime immunization followed by intranasal boost with PLGA microparticles containing RBD/Riboxxim. Antibody responses were assessed by enzyme-linked immunosorbent assay (ELISA), neutralization by competitive ELISA and T-cell responses by enzyme-linked immune spot assay, intracellular cytokine staining and flow cytometry. Memory responses were evaluated 30 days post boost immunization.
Key Results
Vaccination induced robust RBD-specific IgG and IgA antibody titres in both serum and bronchoalveolar lavage fluid, with neutralizing capacity against the Wuhan-Hu-1 strain. Strong CD4+ and CD8+ T-cell responses were detected systemically and in the respiratory tract. Importantly, the vaccine generated durable immunological memory, including tissue-resident memory T-cells in the respiratory tract and long-lived IgG and IgA memory B-cells in secondary lymphoid organs.
Conclusions and Implications
PLGA microparticle-based vaccination induces potent systemic and mucosal immune responses against SARS-CoV-2 RBD. This adaptable platform represents a promising approach for mucosal vaccination strategies, with potential for rapid adaptation to emerging variants.},
keywords = {SARS-CoV-2},
pubstate = {published},
tppubtype = {article}
}
Background and Purpose
Current coronavirus disease 2019 (COVID-19) vaccines effectively prevent severe disease but induce primarily systemic immunity without mucosal protection in the respiratory tract, which is mandatory for protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection and the prevention of viral transmission. Vaccination strategies capable of inducing local immunity at the site of infection are therefore needed. Here, we evaluated a poly (lactic-co-glycolic acid) (PLGA) microparticle-based vaccine co-encapsulating the receptor binding domain (RBD) of SARS-CoV-2 Spike protein with the TLR3/RIG-1 agonist Riboxxim, employing a subcutaneous prime and intranasal boost immunization schedule.
Experimental Approach
BALB/c mice received subcutaneous prime immunization followed by intranasal boost with PLGA microparticles containing RBD/Riboxxim. Antibody responses were assessed by enzyme-linked immunosorbent assay (ELISA), neutralization by competitive ELISA and T-cell responses by enzyme-linked immune spot assay, intracellular cytokine staining and flow cytometry. Memory responses were evaluated 30 days post boost immunization.
Key Results
Vaccination induced robust RBD-specific IgG and IgA antibody titres in both serum and bronchoalveolar lavage fluid, with neutralizing capacity against the Wuhan-Hu-1 strain. Strong CD4+ and CD8+ T-cell responses were detected systemically and in the respiratory tract. Importantly, the vaccine generated durable immunological memory, including tissue-resident memory T-cells in the respiratory tract and long-lived IgG and IgA memory B-cells in secondary lymphoid organs.
Conclusions and Implications
PLGA microparticle-based vaccination induces potent systemic and mucosal immune responses against SARS-CoV-2 RBD. This adaptable platform represents a promising approach for mucosal vaccination strategies, with potential for rapid adaptation to emerging variants.
Current coronavirus disease 2019 (COVID-19) vaccines effectively prevent severe disease but induce primarily systemic immunity without mucosal protection in the respiratory tract, which is mandatory for protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection and the prevention of viral transmission. Vaccination strategies capable of inducing local immunity at the site of infection are therefore needed. Here, we evaluated a poly (lactic-co-glycolic acid) (PLGA) microparticle-based vaccine co-encapsulating the receptor binding domain (RBD) of SARS-CoV-2 Spike protein with the TLR3/RIG-1 agonist Riboxxim, employing a subcutaneous prime and intranasal boost immunization schedule.
Experimental Approach
BALB/c mice received subcutaneous prime immunization followed by intranasal boost with PLGA microparticles containing RBD/Riboxxim. Antibody responses were assessed by enzyme-linked immunosorbent assay (ELISA), neutralization by competitive ELISA and T-cell responses by enzyme-linked immune spot assay, intracellular cytokine staining and flow cytometry. Memory responses were evaluated 30 days post boost immunization.
Key Results
Vaccination induced robust RBD-specific IgG and IgA antibody titres in both serum and bronchoalveolar lavage fluid, with neutralizing capacity against the Wuhan-Hu-1 strain. Strong CD4+ and CD8+ T-cell responses were detected systemically and in the respiratory tract. Importantly, the vaccine generated durable immunological memory, including tissue-resident memory T-cells in the respiratory tract and long-lived IgG and IgA memory B-cells in secondary lymphoid organs.
Conclusions and Implications
PLGA microparticle-based vaccination induces potent systemic and mucosal immune responses against SARS-CoV-2 RBD. This adaptable platform represents a promising approach for mucosal vaccination strategies, with potential for rapid adaptation to emerging variants.
Tsuji, Isamu; Okada, Kumiko; Kroppen, Benjamin; Katta, Tetsufumi; Yamamura, Kaori; Nishihama, Takeshi; Miura, Ayako; Götzke, Hansjörg; Crampon, Eric; Bertolotti-Ciarlet, Andrea
Discovery of Anti-SARS-CoV-2 XBB.1.5 and JN.1 Variant-Specific Monoclonal Single-Domain Antibodies from a Synthetic Library Journal Article
In: Antibodies, vol. 15, no. 2, 2026, ISSN: 2073-4468.
Abstract | Links | Tags: antibody, monoclonal antibody, SARS-CoV-2, vaccine
@article{Tsuji2026,
title = {Discovery of Anti-SARS-CoV-2 XBB.1.5 and JN.1 Variant-Specific Monoclonal Single-Domain Antibodies from a Synthetic Library},
author = {Isamu Tsuji and Kumiko Okada and Benjamin Kroppen and Tetsufumi Katta and Kaori Yamamura and Takeshi Nishihama and Ayako Miura and Hansjörg Götzke and Eric Crampon and Andrea Bertolotti-Ciarlet},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service},
doi = {10.3390/antib15020018},
issn = {2073-4468},
year = {2026},
date = {2026-02-24},
urldate = {2026-02-24},
journal = {Antibodies},
volume = {15},
number = {2},
publisher = {MDPI AG},
abstract = {Background/Objectives:
The SARS-CoV-2 virus frequently undergoes mutations to evade the human immune system. Vaccines for new strains are developed each season, and an identification test confirming the specific strain is essential for vaccine quality control, as stated by the U.S. Food and Drug Administration. However, a shorter timeline of antibody discovery was required to adjust vaccine development schedules. Therefore, anti-SARS-CoV-2 strain-specific, single-domain antibodies (sdAbs) for SARS-CoV-2 vaccines were discovered using alpaca synthetic libraries without animal immunization.
Methods
A synthetic sdAb library was developed based on conserved alpaca sdAb frameworks, with a degree of freedom in the three complementarity-determining regions. Specific and high-affinity sdAb clones were selected from the library by one ribosomal display round, followed by two phage display selections using a biotinylated strain-specific SARS-CoV-2 receptor-binding domain (RBD) of the spike protein as bait and non-biotinylated RBD variants to block. The sdAbs clones were applied to the identification test using Western blotting. The binding epitopes were determined by hydrogen–deuterium exchange mass spectrometry.
Results
Five clones of XBB.1.5 and two clones of JN.1-specific sdAbs were discovered. Anti-JN.1 sdAb clone 1B9 detected JN.1 vaccine products but no other previously produced vaccine strains, Wuhan, BA.5 and XBB.1.5, by WB for vaccine identification test. Four binding epitopes for anti-JN.1 sdAb clone 1B9 were identified, including the L455S mutation, a critical amino acid to evade neutralizing antibodies for the JN.1 strain.
Conclusions
Anti-XBB.1.5 and JN.1-specific sdAbs were discovered from a synthetic single-domain antibody library within 8–9 weeks, and these sdAbs were applied to vaccine identification testing},
keywords = {antibody, monoclonal antibody, SARS-CoV-2, vaccine},
pubstate = {published},
tppubtype = {article}
}
Background/Objectives:
The SARS-CoV-2 virus frequently undergoes mutations to evade the human immune system. Vaccines for new strains are developed each season, and an identification test confirming the specific strain is essential for vaccine quality control, as stated by the U.S. Food and Drug Administration. However, a shorter timeline of antibody discovery was required to adjust vaccine development schedules. Therefore, anti-SARS-CoV-2 strain-specific, single-domain antibodies (sdAbs) for SARS-CoV-2 vaccines were discovered using alpaca synthetic libraries without animal immunization.
Methods
A synthetic sdAb library was developed based on conserved alpaca sdAb frameworks, with a degree of freedom in the three complementarity-determining regions. Specific and high-affinity sdAb clones were selected from the library by one ribosomal display round, followed by two phage display selections using a biotinylated strain-specific SARS-CoV-2 receptor-binding domain (RBD) of the spike protein as bait and non-biotinylated RBD variants to block. The sdAbs clones were applied to the identification test using Western blotting. The binding epitopes were determined by hydrogen–deuterium exchange mass spectrometry.
Results
Five clones of XBB.1.5 and two clones of JN.1-specific sdAbs were discovered. Anti-JN.1 sdAb clone 1B9 detected JN.1 vaccine products but no other previously produced vaccine strains, Wuhan, BA.5 and XBB.1.5, by WB for vaccine identification test. Four binding epitopes for anti-JN.1 sdAb clone 1B9 were identified, including the L455S mutation, a critical amino acid to evade neutralizing antibodies for the JN.1 strain.
Conclusions
Anti-XBB.1.5 and JN.1-specific sdAbs were discovered from a synthetic single-domain antibody library within 8–9 weeks, and these sdAbs were applied to vaccine identification testing
The SARS-CoV-2 virus frequently undergoes mutations to evade the human immune system. Vaccines for new strains are developed each season, and an identification test confirming the specific strain is essential for vaccine quality control, as stated by the U.S. Food and Drug Administration. However, a shorter timeline of antibody discovery was required to adjust vaccine development schedules. Therefore, anti-SARS-CoV-2 strain-specific, single-domain antibodies (sdAbs) for SARS-CoV-2 vaccines were discovered using alpaca synthetic libraries without animal immunization.
Methods
A synthetic sdAb library was developed based on conserved alpaca sdAb frameworks, with a degree of freedom in the three complementarity-determining regions. Specific and high-affinity sdAb clones were selected from the library by one ribosomal display round, followed by two phage display selections using a biotinylated strain-specific SARS-CoV-2 receptor-binding domain (RBD) of the spike protein as bait and non-biotinylated RBD variants to block. The sdAbs clones were applied to the identification test using Western blotting. The binding epitopes were determined by hydrogen–deuterium exchange mass spectrometry.
Results
Five clones of XBB.1.5 and two clones of JN.1-specific sdAbs were discovered. Anti-JN.1 sdAb clone 1B9 detected JN.1 vaccine products but no other previously produced vaccine strains, Wuhan, BA.5 and XBB.1.5, by WB for vaccine identification test. Four binding epitopes for anti-JN.1 sdAb clone 1B9 were identified, including the L455S mutation, a critical amino acid to evade neutralizing antibodies for the JN.1 strain.
Conclusions
Anti-XBB.1.5 and JN.1-specific sdAbs were discovered from a synthetic single-domain antibody library within 8–9 weeks, and these sdAbs were applied to vaccine identification testing
2025
Diaz, Marilyn; Mikulski, Zbignew; Leaman, Dan; Gandarilla, Angel; Silva, Nathalia Da; Verkoczy, Annie; Zhang, Jinsong; Verkoczy, Laurent
In: Front. Immunol., vol. 16, 2025, ISSN: 1664-3224.
Abstract | Links | Tags: P2020-022, P2020-029, SARS-CoV-2
@article{Diaz2025,
title = {SARS-CoV-2 spike peptide analysis reveals a highly conserved region that elicits potentially pathogenic autoantibodies: implications to pan-coronavirus vaccine development},
author = {Marilyn Diaz and Zbignew Mikulski and Dan Leaman and Angel Gandarilla and Nathalia Da Silva and Annie Verkoczy and Jinsong Zhang and Laurent Verkoczy},
url = {https://trenzyme.com/protein-production-services/custom-protein-expression-service/, ➥Custom Protein Expression Service
https://trenzyme.shop/products/spike-s1-rbd-tag-free, ➥Mentioned protein in trenzyme webshop (SKU P2020-022)
https://trenzyme.shop/products/s-protein-trimer-tag-removed, ➥Mentioned protein in trenzyme webshop (SKU P2020-029)},
doi = {10.3389/fimmu.2025.1488388},
issn = {1664-3224},
year = {2025},
date = {2025-02-25},
urldate = {2025-02-25},
journal = {Front. Immunol.},
volume = {16},
publisher = {Frontiers Media SA},
abstract = {The SARS-CoV-2 pandemic, while subsiding, continues to plague the world as new variants emerge. Millions have died, and millions more battle with the debilitating symptoms of a clinical entity known as long Covid. The biggest challenge remains combating an ever-changing variant landscape that threatens immune evasion from vaccine and prior infection-generated immunity. In addition, the sequelae of symptoms associated with long Covid almost certainly point to multiple pathologies that range from direct damage to organs during infection to a potential role for infection-induced autoreactive antibodies in promoting autoimmune-like conditions in these patients. In this study, a peptide scan of the SARS-CoV-2 spike protein was done to detect novel, highly conserved linear epitopes that do not elicit autoantibodies. We identified eight predicted linear epitopes capable of eliciting anti-spike IgG antibodies. Immunizations alternating peptide conjugated to KLH with the full trimer yielded the highest antibody levels, but homologous immunization with some of the peptides also yielded high levels when an additional immunization step was added. Of all regions tested, the stem helix adjacent to the heptad repeat 2 (HR2) region also elicited high levels of autoreactive antibodies to known autoantigens in common systemic autoimmune disorders such as lupus and scleroderma and may contribute to the long Covid syndrome seen in some patients. Implications to vaccine design are discussed.},
keywords = {P2020-022, P2020-029, SARS-CoV-2},
pubstate = {published},
tppubtype = {article}
}
The SARS-CoV-2 pandemic, while subsiding, continues to plague the world as new variants emerge. Millions have died, and millions more battle with the debilitating symptoms of a clinical entity known as long Covid. The biggest challenge remains combating an ever-changing variant landscape that threatens immune evasion from vaccine and prior infection-generated immunity. In addition, the sequelae of symptoms associated with long Covid almost certainly point to multiple pathologies that range from direct damage to organs during infection to a potential role for infection-induced autoreactive antibodies in promoting autoimmune-like conditions in these patients. In this study, a peptide scan of the SARS-CoV-2 spike protein was done to detect novel, highly conserved linear epitopes that do not elicit autoantibodies. We identified eight predicted linear epitopes capable of eliciting anti-spike IgG antibodies. Immunizations alternating peptide conjugated to KLH with the full trimer yielded the highest antibody levels, but homologous immunization with some of the peptides also yielded high levels when an additional immunization step was added. Of all regions tested, the stem helix adjacent to the heptad repeat 2 (HR2) region also elicited high levels of autoreactive antibodies to known autoantigens in common systemic autoimmune disorders such as lupus and scleroderma and may contribute to the long Covid syndrome seen in some patients. Implications to vaccine design are discussed.
Vázquez-Díaz, Silvia; Saa, Laura; Otaegui, David; Pavlov, Valeri; Palazón, Asis; Cortajarena, Aitziber L.
In: Anal. Chem., vol. 97, no. 6, pp. 3361–3370, 2025, ISSN: 1520-6882.
Abstract | Links | Tags: Au/Pt NCs-IgG, P2020-001, P2020-100, SARS-CoV-2
@article{Vázquez-Díaz2025,
title = {Dual-Mode Immunosensor for Antibody Detection: Harnessing the Versatility of Antibody-Based Nanozymes across Optical and Electrochemical Platforms},
author = {Silvia Vázquez-Díaz and Laura Saa and David Otaegui and Valeri Pavlov and Asis Palazón and Aitziber L. Cortajarena},
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)
https://trenzyme.shop/products/influenza-a-g4-ea-h1n1-ha1, ➥Mentioned protein in trenzyme webshop (SKU P2020-100)},
doi = {10.1021/acs.analchem.4c05317},
issn = {1520-6882},
year = {2025},
date = {2025-02-18},
urldate = {2025-02-18},
journal = {Anal. Chem.},
volume = {97},
number = {6},
pages = {3361--3370},
publisher = {American Chemical Society (ACS)},
abstract = {In the early years of the 21st century, numerous viral infectious diseases have proliferated, prompting intensified efforts to devise more effective diagnostic methods. In response, various biosensors have emerged with the aim of overcoming the constraints of conventional diagnostic techniques. Nanomaterial-based biosensors have revolutionized conventional approaches, significantly enhancing biosensor performance and effectively tackling these challenges. A diverse array of nanoparticles and nanomaterials has been systematically synthesized, engineered, and employed to augment the functionalities of biosensors. This work capitalizes on the properties of gold–platinum bimetallic nanoclusters (NCs) embedded in the structure of an immunoglobulin (IgG) (Au/Pt NCs-IgG), unveiling a novel double strategy for the detection of antibodies that leverages both their catalytic NC scaffold and the biorecognition element. The detection mechanism revealed the unique oxidase-like properties of Au/Pt NCs-IgG. This distinctive property, in addition to previously reported peroxidase-like activity, positions Au/Pt NCs-IgG as an effective probe in both optical and electrochemical sandwich enzyme-linked immunosorbent assays, facilitating their incorporation in different sensor frameworks and their utilization across various applications. As a study case, anti-SARS-CoV-2 antibodies (anti-RBD IgG antibodies) were employed as the target analyte. A linear detection range was found between 0.5 and 100 ng/mL for optical immunosensors and 50–300 ng/mL for electrochemical immunosensors. The validation of the immunosensor in clinical samples demonstrated its promising diagnostic value. The significantly differential signal obtained between positive and negative clinical samples underscores the suitability of both sensors for point-of-care diagnostic applications.},
keywords = {Au/Pt NCs-IgG, P2020-001, P2020-100, SARS-CoV-2},
pubstate = {published},
tppubtype = {article}
}
In the early years of the 21st century, numerous viral infectious diseases have proliferated, prompting intensified efforts to devise more effective diagnostic methods. In response, various biosensors have emerged with the aim of overcoming the constraints of conventional diagnostic techniques. Nanomaterial-based biosensors have revolutionized conventional approaches, significantly enhancing biosensor performance and effectively tackling these challenges. A diverse array of nanoparticles and nanomaterials has been systematically synthesized, engineered, and employed to augment the functionalities of biosensors. This work capitalizes on the properties of gold–platinum bimetallic nanoclusters (NCs) embedded in the structure of an immunoglobulin (IgG) (Au/Pt NCs-IgG), unveiling a novel double strategy for the detection of antibodies that leverages both their catalytic NC scaffold and the biorecognition element. The detection mechanism revealed the unique oxidase-like properties of Au/Pt NCs-IgG. This distinctive property, in addition to previously reported peroxidase-like activity, positions Au/Pt NCs-IgG as an effective probe in both optical and electrochemical sandwich enzyme-linked immunosorbent assays, facilitating their incorporation in different sensor frameworks and their utilization across various applications. As a study case, anti-SARS-CoV-2 antibodies (anti-RBD IgG antibodies) were employed as the target analyte. A linear detection range was found between 0.5 and 100 ng/mL for optical immunosensors and 50–300 ng/mL for electrochemical immunosensors. The validation of the immunosensor in clinical samples demonstrated its promising diagnostic value. The significantly differential signal obtained between positive and negative clinical samples underscores the suitability of both sensors for point-of-care diagnostic applications.
Mosca, Andrea; Arsene, Cristian-Gabriel; Paleari, Renata; Kaiser, Patricia; Harteveld, Kees; Daniel, Yvonne; Amano, Chie; Murakami, Atsushi; Auclair, Guy
Standardization of hemoglobin A2 and hemoglobin F: Achievements and perspectives Journal Article
In: Clinica Chimica Acta, vol. 567, 2025, ISSN: 0009-8981.
Abstract | Links | Tags: HbA2, HbF, P2020-193, P2020-199
@article{Mosca2025,
title = {Standardization of hemoglobin A2 and hemoglobin F: Achievements and perspectives},
author = {Andrea Mosca and Cristian-Gabriel Arsene and Renata Paleari and Patricia Kaiser and Kees Harteveld and Yvonne Daniel and Chie Amano and Atsushi Murakami and Guy Auclair},
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)
https://shop.trenzyme.com/products/hemoglobin-hbf-%CE%B12-%CE%B32, ➥Mentioned protein in trenzyme webshop (SKU P2020-199)},
doi = {10.1016/j.cca.2024.120087},
issn = {0009-8981},
year = {2025},
date = {2025-02-00},
urldate = {2025-02-00},
journal = {Clinica Chimica Acta},
volume = {567},
publisher = {Elsevier BV},
abstract = {The establishment of reference systems for the standardization of hemoglobin A2 (HbA2) and fetal hemoglobin (HbF), both critical for improving diagnostic accuracy in conditions such as β-thalassemia and sickle cell disease, are described. Efforts were led by the IFCC and other groups to address and reduce the variability in laboratory measurements of these hemoglobins. This document outlines the production of certified reference materials (CRMs) for HbA2 and the development of a reference measurement procedure using isotope dilution mass spectrometry. Similarly, standardizing HbF is essential for supporting diagnostic and therapeutic strategies, particularly in managing sickle cell disease. HbF levels can predict disease outcomes and guide treatment plans. Significant challenges remain in achieving consistent measurement across laboratories, and the process for standardization for this minor hemoglobin has just begun. We are confident that the implementation of these reference systems will provide improved accuracy and traceability in the future.},
keywords = {HbA2, HbF, P2020-193, P2020-199},
pubstate = {published},
tppubtype = {article}
}
The establishment of reference systems for the standardization of hemoglobin A2 (HbA2) and fetal hemoglobin (HbF), both critical for improving diagnostic accuracy in conditions such as β-thalassemia and sickle cell disease, are described. Efforts were led by the IFCC and other groups to address and reduce the variability in laboratory measurements of these hemoglobins. This document outlines the production of certified reference materials (CRMs) for HbA2 and the development of a reference measurement procedure using isotope dilution mass spectrometry. Similarly, standardizing HbF is essential for supporting diagnostic and therapeutic strategies, particularly in managing sickle cell disease. HbF levels can predict disease outcomes and guide treatment plans. Significant challenges remain in achieving consistent measurement across laboratories, and the process for standardization for this minor hemoglobin has just begun. We are confident that the implementation of these reference systems will provide improved accuracy and traceability in the future.
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2024:
