Analyzing Fcγ-Receptor Interactions on Monocytes with the Proximity Ligation Assay (PLA)

Sibel Kara; Falk Nimmerjahn

doi:10.1007/978-1-0716-3437-0_26

Analyzing Fcγ-Receptor Interactions on Monocytes with the Proximity Ligation Assay (PLA)

Methods Mol Biol. 2024:2713:377-388. doi: 10.1007/978-1-0716-3437-0_26.

Authors

Sibel Kara¹, Falk Nimmerjahn²

Affiliations

¹ Division of Genetics, Department of Biology, University of Erlangen-Nürnberg, Erlangen, Germany.
² Division of Genetics, Department of Biology, University of Erlangen-Nürnberg, Erlangen, Germany. falk.nimmerjahn@fau.de.

PMID: 37639137
DOI: 10.1007/978-1-0716-3437-0_26

Abstract

Proximity ligation assays (PLA) enable the detection and characterization of protein interactions independent of protein abundance or genetic modifications. This technique exploits both antibody and DNA-binding features, providing high selectivity and sensitivity for protein recognition and visualization of single-protein molecules with high spatial accuracy. Here, we describe the general procedure for a direct PLA on splenic monocytes to analyze FcγRIIb homodimerization. However, this method can be applied to other cells and receptors of interest.

Keywords: Antibody; Fc receptor; Microscopy; Protein interaction; Proximity ligation assay (PLA).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Antibodies
Gene Editing
Monocytes*
Receptors, IgG*
Spleen

Substances

Receptors, IgG
Antibodies