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Differential binding of anti-Reelin monoclonal antibodies reveals the characteristics of Reelin protein under various conditions.

Authors
  • Ishii, Keisuke1
  • Kohno, Takao1
  • Hattori, Mitsuharu2
  • 1 Department of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, 467-8603, Japan. , (Japan)
  • 2 Department of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, 467-8603, Japan. Electronic address: [email protected] , (Japan)
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier
Publication Date
Jun 30, 2019
Volume
514
Issue
3
Pages
815–820
Identifiers
DOI: 10.1016/j.bbrc.2019.05.005
PMID: 31079931
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Reelin is a large secreted protein that is essential for the development and function of the central nervous system. Dimerization and/or oligomerization is required for its biological activity, but the underlying mechanism is not fully understood. There are several widely used anti-Reelin antibodies and we noticed that their reactivity to monomeric or dimeric Reelin protein is different. We also found that their reactivity to Reelin in the solution or in fixed brain tissues also differs. Our results provide the information regarding how the N-terminal region of Reelin folds and contributes to the formation of higher order structure. We also provide a caveat that appropriate use of anti-Reelin antibody is necessary for quantitative analyses. Copyright © 2019 Elsevier Inc. All rights reserved.

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