New Citations in January 2026
At the start of 2026, multiple AntibodySystem products were cited in peer-reviewed publications across leading international journals, including Microbiology Spectrum, MedComm, ACS Applied Materials & Interfaces, Journal of Virology, and others. These studies span diverse research areas such as viral pathogenesis, mRNA vaccine development, extracellular vesicle (EV) detection technologies, autoimmune disease mechanisms, and fluorescence-guided cancer imaging.
Together, these publications underscore the value of AntibodySystem reagents in multidisciplinary research—supporting everything from molecular target validation to translational diagnostics and therapeutic innovation.
1. MedComm (IF 10.7)
An mRNA Vaccine Based on Antigens From Conserved Regions of Monkeypox Virus A35R and M1R With a Dimer-Like Conformation Confers Protection Against Both Monkeypox Virus and Vaccinia Virus Infections in Mice
PMID: 41583908
Study Overview: In response to the 2022 monkeypox outbreak, this study designed four mRNA vaccine candidates based on conserved regions of the MPXV A35R and M1R antigens. In murine models, dual-antigen vaccines (MV1 and MV2) elicited stronger immunogenicity compared to single-antigen formulations. Notably, MV2—engineered using AlphaFold3 to adopt a dimer-like conformation—demonstrated superior protective efficacy and induced durable immunity against both monkeypox virus and vaccinia virus, highlighting its potential as a clinical vaccine candidate.
Products Cited:
Recombinant Monkeypox virus/MPXV M1R Protein, C-His (EVV13301)
Recombinant Monkeypox virus/MPXV A35R Protein, C-His (EVV13101)
Application: The Recombinant Monkeypox virus/MPXV M1R Protein, C-His (EVV13301) and Recombinant Monkeypox virus/MPXV A35R Protein, C-His (EVV13101) were used as coating antigens in ELISA assays to quantify antigen-specific IgG titers in sera from immunized mice. The data enabled comparative evaluation of humoral immune responses elicited by different mRNA vaccine candidates and provided critical evidence supporting the selection of optimized dual-antigen constructs.
2. ACS Appl Mater Interfaces (IF 8.2)
Ultrabright Carbon Dots as an Emerging Fluorescent Probe for Multivalent Labeling and Highly Sensitive Detection of Extracellular Vesicles
PMID: 41553826
Study Overview: To address limitations of conventional EV fluorescent probes, researchers developed cholesterol-modified ultrabright green carbon dots (Chol-GCDs) with high quantum yield and enhanced photostability. Integrated into a 96-well sandwich assay platform, the system enabled quantitative detection of EVs within a dynamic range of 10³–10⁶ particles/mL and demonstrated robust analytical performance in serum and cell culture supernatants.
Product Cited: Anti-Human CD81 Antibody (005-C01) (RHF34001)
Application: The Anti-Human CD81 Antibody (005-C01) (RHF34001) served as the capture antibody in the sandwich fluorescence assay, enabling selective binding of CD81-positive EVs. Its use facilitated efficient EV capture and quantification, supporting the development of a highly sensitive and specific EV detection platform for biological samples.
3. Int Immunopharmacol (IF 4.7)
Targeting the MDSC-Th17 axis: Sinomenine suppresses rheumatoid arthritis by disrupting arginase-1-mediated immune crosstalk
PMID: 41483617
Study Overview: This study elucidates the immunomodulatory mechanism of sinomenine in rheumatoid arthritis (RA). The compound was shown to directly bind JAK1, suppressing the IL-6/JAK1/STAT3 signaling pathway and downregulating Arg1 expression in myeloid-derived suppressor cells (MDSCs). This disruption of MDSC-mediated Th17 polarization attenuated disease progression. MDSC depletion abolished the therapeutic effect, confirming MDSCs as a key target.
Product Cited: Recombinant Human JAK1 Protein, N-His (YHD57901)
Application: The Recombinant Human JAK1 Protein, N-His (YHD57901) was used in molecular docking validation and surface plasmon resonance (SPR) assays to confirm the direct interaction between sinomenine and JAK1, providing mechanistic insight into pathway inhibition and downstream immune modulation.
4. Molecular Pharmaceutics (IF 4.5)
Indocyanine Green-Labeled Antibodies Cotargeting CDCP1 and Mesothelin for Fluorescence-Guided Imaging of Pancreatic Cancer
PMID: 41553332
Study Overview: Pancreatic ductal adenocarcinoma (PDAC) remains highly lethal. This study conjugated indocyanine green (ICG) to anti-CDCP1 (ch10D7) and anti-mesothelin (amatuximab) antibodies. Both retained high affinity and specificity. In subcutaneous and orthotopic PDAC mouse models, dual targeting significantly enhanced tumor fluorescence signals, with peak imaging at 120 hours post-administration. CRISPR knockout of target antigens abolished fluorescence, confirming specificity.
Product Cited: Anti-Human MSLN Antibody (SAA0145), PE (FHG52012)
Application: The Anti-Human MSLN Antibody (SAA0145), PE (FHG52012) was used in flow cytometry to quantify mesothelin expression on PDAC cell lines (HPAF-II and TKCC10). By calibrating against PE standard beads, researchers estimated antigen density per cell, providing critical quantitative data to guide subsequent ICG-based targeting and imaging studies.
5. Virus Evolution (IF 4.0)
The S190R mutation in RSV-A F protein impairs nirsevimab binding and neutralization capacity
PMID: 41660179
Study Overview: Nirsevimab is an approved monoclonal antibody for RSV prophylaxis in infants. This study identified an S190R mutation in the RSV-A F protein that reduces nirsevimab binding and neutralization by decreasing epitope accessibility at antigenic site Ø. However, the mutation compromised viral fitness, limiting replication in cell lines, human nasal organoids, and mouse models.
Product Cited: Anti-HRSV-A F/Fusion glycoprotein F0 Antibody (D25) (RVV02809)
Application: The Anti-HRSV-A F/Fusion glycoprotein F0 Antibody (D25) (RVV02809) was used in flow cytometry to assess surface antigen accessibility on HEp-2 cells infected with wild-type or S190R mutant RSV-A. Comparative analysis with antibodies targeting alternative antigenic sites clarified the structural impact of the mutation on site Ø exposure.
6. Journal of Virology (IF 3.8)
Cell-cell fusion limits activation of the unfolded protein response induced by the Nipah virus glycoproteins
PMID: 41378893
Study Overview: Nipah virus (NiV) glycoprotein synthesis in host cells may induce endoplasmic reticulum (ER) stress and activate the unfolded protein response (UPR). This study demonstrated that NiV F and G glycoproteins activate the IRE1/XBP1 UPR pathway individually; however, their co-expression promotes cell–cell fusion, which paradoxically limits UPR activation. Fusion efficiency was inversely correlated with UPR signaling, suggesting a dilution mechanism that balances viral propagation with avoidance of excessive ER stress.
Products Cited:
Anti-Nipah virus/HeV F/Fusion glycoprotein F0 Polyclonal Antibody (PVV08101)
Anti-Nipah virus/HeV G protein/Glycoprotein G Polyclonal Antibody (PVV07901)
Application: The Anti-Nipah virus/HeV F/Fusion glycoprotein F0 Polyclonal Antibody (PVV08101) and Anti-Nipah virus/HeV G protein/Glycoprotein G Polyclonal Antibody (PVV07901) were used in Western blot analysis to detect expression levels of NiV F and G glycoproteins in Vero76 cells. The data supported mechanistic investigation into how glycoprotein expression and cell fusion modulate UPR activation.
7. Microbiology Spectrum (IF 3.8)
New insight into the epidemiological trends of respiratory syncytial virus infection and the underlying anti-respiratory syncytial virus mechanisms of andrographolide: integrating Global Burden of Disease database, network pharmacological analysis, and in vitro experiments
PMID: 41230964
Study Overview: This study integrated Global Burden of Disease data, network pharmacology, and in vitro experiments to examine RSV epidemiology and evaluate andrographolide as a candidate antiviral agent. Andrographolide demonstrated superior anti-RSV activity compared to ribavirin. Mechanistically, it competitively binds the host receptor CX3CR1 to inhibit viral attachment and modulates the ROS/TXNIP/NF-κB pathway to suppress RSV-induced oxidative stress and inflammatory cytokine production.
Product Cited: Anti-HRSV F Protein Antibody (131-2A) (RVV02818)
Application: The Anti-HRSV F Protein Antibody (131-2A) (RVV02818) was employed in immunofluorescence assays to detect RSV F protein expression on HEp-2 cells, supporting evaluation of viral adsorption, replication, and proliferation following andrographolide treatment.
Conclusion · Empowering Global Discovery
AntibodySystem remains committed to empowering fundamental research and translational innovation worldwide—providing reliable, high-quality reagents that accelerate scientific discovery across life sciences.
