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Related Experiment Video

Updated: Aug 9, 2025

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

The lamin A/C Ig-fold undergoes cell density-dependent changes that alter epitope binding.

Melanie Wallace^1,2, Gregory R Fedorchak^1,2, Richa Agrawal^1,2

¹Meinig School of Biomedical Engineering, Cornell University, Ithaca, NY, USA.

Nucleus (Austin, Tex.)

|February 22, 2023

Summary

Antibody recognition of Lamins A/C changes with cell density due to conformational shifts, not protein levels. This impacts immunofluorescence data interpretation for nuclear intermediate filament proteins.

Keywords:

Ig-fold Lamins cell density cell spreading immunofluorescence immunolabeling lamin A lamin A/C lamin C mechanobiology nuclear envelope

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Last Updated: Aug 9, 2025

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

Cell Biology
Biochemistry
Biophysics

Background:

Lamins A/C are nuclear intermediate filament proteins crucial for cellular mechanics and biochemistry.
Antibody-based detection is vital for studying Lamin A/C localization and function.

Purpose of the Study:

To investigate the cell density-dependent recognition of Lamins A/C by antibodies.
To understand the underlying mechanisms and implications for immunofluorescence studies.

Main Methods:

Immunofluorescence using JOL-2 antibody targeting Lamin A/C Ig-fold.
Cell density manipulation and cell spreading assays.
Cytoskeletal disruption and Linker of Nucleoskeleton and Cytoskeleton (LINC) complex perturbation.
Nuclear stiffness and force transmission measurements.

Main Results:

Antibody JOL-2 recognition of Lamin A/C is highly dependent on cell density, despite unchanged Lamin A/C levels.
Proposed mechanism involves conformational changes (unfolding/masking) of Ig-fold loops (C'E, EF) upon cell spreading.
Labeling was unaffected by cytoskeletal or LINC complex disruption.
Nuclear stiffness and force transmission remained constant across cell densities.

Conclusions:

Cell density influences Lamin A/C antibody accessibility, likely via conformational changes.
Findings necessitate careful interpretation of immunofluorescence data for Lamins A/C.
Conformational plasticity of Lamins A/C may be functionally relevant in cellular processes.