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Welch NG, Scoble JA, Easton CD, et al. High-Throughput Production of Chromium(III) Complexes for Antibody Immobilization. Anal Chem. 2016;88(20):10102-10110doi: 10.1021/acs.analchem.6b02531.
Welch, N. G., Scoble, J. A., Easton, C. D., Williams, C. C., Bradford, B. J., Mamedova, L. K., Pigram, P. J., & Muir, B. W. (2016). High-Throughput Production of Chromium(III) Complexes for Antibody Immobilization. Analytical chemistry, 88(20), 10102-10110. https://doi.org/10.1021/acs.analchem.6b02531
Welch, Nicholas G, et al. "High-Throughput Production of Chromium(III) Complexes for Antibody Immobilization." Analytical chemistry vol. 88,20 (2016): 10102-10110. doi: https://doi.org/10.1021/acs.analchem.6b02531
Welch NG, Scoble JA, Easton CD, Williams CC, Bradford BJ, Mamedova LK, Pigram PJ, Muir BW. High-Throughput Production of Chromium(III) Complexes for Antibody Immobilization. Anal Chem. 2016 Oct 18;88(20):10102-10110. doi: 10.1021/acs.analchem.6b02531. Epub 2016 Oct 05. PMID: 27644116.
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Anal Chem. 2016 Oct 18;88(20):10102-10110. doi: 10.1021/acs.analchem.6b02531. Epub 2016 Oct 05.

High-Throughput Production of Chromium(III) Complexes for Antibody Immobilization.

Analytical chemistry

Nicholas G Welch, Judith A Scoble, Christopher D Easton, Charlotte C Williams, Barry J Bradford, Laman K Mamedova, Paul J Pigram, Benjamin W Muir

Affiliations

  1. Centre for Materials and Surface Science and Department of Chemistry and Physics, La Trobe University , Bundoora, Victoria 3086, Australia.
  2. CSIRO, Manufacturing, Clayton, Victoria 3168, Australia.
  3. Kansas State University , Department of Animal Sciences and Industry, Manhattan, Kansas 66506, United States.

PMID: 27644116 DOI: 10.1021/acs.analchem.6b02531

Abstract

A robot-assisted high-throughput methodology was employed to produce chromium(III) complexes suitable for the surface modification of the commercially available PerkinElmer Optiplate96 well plate for use in enzyme-linked immunosorbent assays (ELISAs). The complexes were immobilized to the native functionality of the well plate and first screened using a horseradish-peroxidase-tagged (HRP) mouse antibody to quantify binding. The top "hits" were further assessed for their ability to present the antibody in a functional state using an ELISA. "Hits" from the second screen yielded four complexes capable of improving the signal intensity of the ELISA by greater than 500%. The metal/base ratio of these complexes was also investigated, and we isolated the most stable and reproducible candidate, [Cr(OH)

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