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Immunoprecipitation

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: May 27, 2026

Preparation of Synaptoneurosomes from Mouse Cortex using a Discontinuous Percoll-Sucrose Density Gradient

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Published on: September 17, 2011

Protein composition of immunoprecipitated synaptic ribbons.

A Kantardzhieva¹, M Peppi, W S Lane

¹Eaton-Peabody Laboratory, Department of Otology and Laryngology, Massachusetts Eye and Ear Infirmary and Harvard Medical School, 243 Charles Street, Boston, Massachusetts 02114, United States.

Journal of Proteome Research

|November 23, 2011

Summary

Researchers quantified the protein composition of the synaptic ribbon complex in sensory cells. This analysis revealed 30 associated proteins, crucial for vesicle handling and neurotransmitter release.

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Subcellular Fractionation for the Isolation of Synaptic Components from the Murine Brain

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Related Experiment Videos

Last Updated: May 27, 2026

Preparation of Synaptoneurosomes from Mouse Cortex using a Discontinuous Percoll-Sucrose Density Gradient

Preparation of Synaptoneurosomes from Mouse Cortex using a Discontinuous Percoll-Sucrose Density Gradient

Published on: September 17, 2011

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

Subcellular Fractionation for the Isolation of Synaptic Components from the Murine Brain

Subcellular Fractionation for the Isolation of Synaptic Components from the Murine Brain

Published on: September 14, 2022

Area of Science:

Neuroscience
Cell Biology
Proteomics

Background:

The synaptic ribbon is a specialized structure in sensory hair cells and photoreceptors.
It plays a critical role in neurotransmitter vesicle release, essential for signal transduction.

Purpose of the Study:

To objectively and quantitatively analyze the protein composition of the synaptic ribbon complex.
To identify proteins associated with the ribbon and understand their functional roles.

Main Methods:

Mass spectrometry-based proteomics was employed for comprehensive protein identification.
Affinity purification of synaptic ribbons and control immunoprecipitations were used to ensure specificity.
Analysis was performed on mouse tissue for a complete proteomic profile.

Main Results:

Thirty proteins, including 56 isoforms and subunits, were identified as associated with the synaptic ribbon complex.
Proteins were categorized into functional groups: vesicle handling (38.5%), scaffold (7.3%), cytoskeletal molecules (20.6%), phosphorylation enzymes (10.6%), molecular chaperones (8.2%), and transmembrane proteins (11.3%).
The three CtBP isoforms were identified as the most abundant proteins within the ribbon complex.

Conclusions:

The synaptic ribbon complex is composed of proteins involved in vesicle dynamics and exocytosis.
A significant presence of phosphorylation enzymes suggests a highly regulated and active structure.
The findings provide a comprehensive understanding of the molecular architecture and function of the synaptic ribbon.