Evidence map›Paper›PMID 40503728›Full record

ArticleBioanalysis2025

The case for calibration-free concentration analysis.

Shannon D Chilewski

Abstract read
In one paragraph

Article in Bioanalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Shannon D ChilewskiBristol Myers Squibb, Precision Medicine, Bioanalytical, and Translational Sciences, Princeton, NJ, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accurate measurement of protein concentration is crucial in biological research, where protein-based reagents play a key role in assay performance and reliability. Traditional methods of protein quantification often measure total protein concentration, failing to account for the active portion capable of binding to its intended target. Calibration-free concentration analysis (CFCA), which uses surface plasmon resonance (SPR) technology, offers a solution by specifically measuring the active protein concentration of the sample. CFCA leverages binding under partially mass-transport limited conditions to directly quantify the functional protein in a sample, overcoming variability associated with recombinant protein production. This article provides a background on CFCA and the case for its more widespread use in protein reagent characterization, as it offers a way to reduce lot-to-lot and vendor-to-vendor variability while improving reproducibility and standardization of assays. This perspective was informed by searching and selecting pertinent articles from PubMed (Nov 2024-March 2025) and by examining the reference lists of key papers.

Indexed as

ProteinsSurface Plasmon ResonanceCalibrationHumansReproducibility of ResultsProteinsbioanalyticalcalibration-free concentration analysisconcentration analysisCritical reagentsligand binding assaysrecombinant proteins

Identifiers

PMID40503728
PMCPMC12203858

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

None linked

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 OpenQuestion graph.