ArticleAnalytical chemistry2026
Overcoming Electrochemiluminescence Immunoassay (ECLIA) Limitations: Conformation-Independent Quantitation of a Therapeutic Antibody by LC-MS/MS.
Article in Analytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Monoclonal antibody therapies have transformed cancer treatment by enabling targeted intervention even in advanced disease stages. However, reliable monitoring of circulating therapeutic antibody levels is critical to ensuring efficacy and patient safety. This study investigates the limitations of an electrochemiluminescence immunoassay (ECLIA) in quantifying a therapeutic immunoglobulin G2 (IgG2) antibody, known to undergo conformational changes in vivo. We observed that the ECLIA failed to reflect increasing antibody concentrations in patient plasma, instead producing a plateau effect. This discrepancy was attributed to the ECLIA's reliance on the intact structural conformation of the antibody, which may be altered during circulation. In contrast, a mass spectrometry (MS)-based approach successfully quantified the accumulating antibody levels over time, independent of conformational state. These findings highlight the need for alternative quantitation strategies in clinical settings, particularly when structural heterogeneity may compromise the ECLIA performance. Mass spectrometry provides a robust and reliable option for monitoring therapeutic antibodies under these conditions.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.