Nuclear Protein Extraction

Nuclear protein extraction is a laboratory method for isolating proteins from cell nuclei, enabling researchers to study gene regulation, chromatin organization, and nuclear signaling. The process typically uses sequential lysis: a mild buffer disrupts the plasma membrane while preserving intact nuclei, followed by nuclear isolation and stronger detergent or high-salt treatment to disrupt the nuclear envelope and release soluble and chromatin-associated proteins. Extracts can be analyzed by Western blotting, immunoprecipitation, or DNA-binding assays to investigate transcription factors, histones, and other nuclear components. This approach supports research in cell biology, development, disease mechanisms, and drug-response studies.

Nuclear Protein Extraction - Related Videos

Research

JoVE Journal - Biology
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In Vitro Nuclear Assembly Using Fractionated Xenopus Egg Extracts

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Cited by 5 •

2008

Nuclear membrane assembly is an essential step in the cell division cycle; this process can be replicated in the test tube by combining Xenopus sperm chromatin, cytosol, and light membrane fractions. Complete nuclei are formed, including nuclear membranes with pore complexes, and these reconstituted nuclei are capable of normal nuclear processes.

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JoVE Journal - Biology
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Small-scale Nuclear Extracts for Functional Assays of Gene-expression Machineries

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Cited by 37 •

2012

A protocol for preparation of robust, small-scale HeLa nuclear extracts is described. This protocol is valuable for assays that require use of small populations of cells, such as cells treated with drugs or RNAi. The method should be applicable to a wide variety of gene expression assays and other cell types, including patient cells.

Research

JoVE Journal - Biochemistry

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

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Cited by 1 •

2017

We have established a method for the purification of coregulatory interaction proteins using the LC-MS/MS system.

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

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Cited by 15 •

2017

Protein-protein interactions can occur in both the nucleus and the cytoplasm of a cell. To investigate these interactions, traditional co-immunoprecipitation and modern proximity ligation assay are applied. In this study, we compare these two methods to visualize the distribution of NF90-RBM3 interactions in the nucleus and the cytoplasm.

A Cell-Free Assay Using Xenopus laevis Embryo Extracts to Study Mechanisms of Nuclear Size Regulation

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Cited by 12 •

2016

Mechanisms of cellular and intra-cellular scaling remain elusive. The use of Xenopus embryo extracts has become increasingly common to elucidate mechanisms of organelle size regulation. This method describes embryo extract preparation and a novel nuclear scaling assay through which mechanisms of nuclear size regulation can be identified.

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