Evidence map›Paper›PMID 31758924›Full record

ArticleAnalytical biochemistry2020

A flexible, robust microbead-based assay for quantification and normalization of target protein concentrations.

Eric J Snider, Alexandra R Crowley, Julia Raykin, R Kijoon Kim, Fiona Splaine, C Ross Ethier

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytical biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Sample Preparation and Protein Determination for 2D-DIGE Proteomics.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  2. Review
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

6 authors.

Eric J SniderWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA.
Alexandra R CrowleyWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA.
Julia RaykinWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA.
R Kijoon KimWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA.
Fiona SplaineWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA.
C Ross EthierWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA, USA. Electronic address: ross.ethier@bme.gatech.edu.

Funding

Targeting Scleral Stiffness as a Novel Therapeutic Approach in GlaucomaR01EY025286 · NEI · GEORGIA INSTITUTE OF TECHNOLOGY · PI ETHIER, C ROSS · 2015 to 2019
$2.5M
NEI NIH HHS R01 EY025286
6 · The paper itself

Abstract

Although there are many methods for quantifying the concentration of specific proteins in samples, current techniques are technically challenging or do not easily lend themselves to normalization. Here, we describe a microbead-based assay for quantifying specific protein concentration(s) that is high-throughput, inexpensive, simple-to-use, and intrinsically incorporates normalization against the sample total protein content. This assay, termed the FRANC assay, exploits high affinity biotin-streptavidin binding to couple sample proteins to streptavidin-labelled magnetic microbeads. Proteins are then antibody-probed, followed by labeling of proteins on the microbead with fluorescent dye, and flow cytometry-based analysis. The FRANC assay demonstrates detection limits for target proteins in the femtogram range, with a linear range up to as much as 10 ng. Normalization of target protein concentrations resulted in an 80% reduction in variability as compared to non-normalized measurements. We conclude that the FRANC assay offers attractive advantages over current methods for quantifying specific protein(s) in samples.

Indexed as

AnimalsBiotinCell Line, TumorFlow CytometryFluorescent DyesGoatsHumansMiceMicrospheresProteinsRabbitsStreptavidinBiotinFluorescent DyesProteinsStreptavidinAssay developmentBiotin-streptavidinFlow cytometryProtein expression

Identifiers

PMID31758924
PMCPMC6934895

What OpenQuestion holds

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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.