Histone chaperones are a group of essential proteins that bind to histones, thereby participating in chromatin condensation and assembly and regulating chromatin function. The study of histone-associated chaperone proteins focuses on the mechanisms by which histones move in and out of the nucleosome and how they are modified by modifying groups. This enables you to understand better how genes are specifically expressed and the impact of these histones and their modifications on genetic information. Lifeasible can characterize histone post-translational modification binding chaperones by a range of methods.

In addition to this, we offer analytical volumetric exclusion chromatography (SEC) to study histone chaperone oligomerization and stability, the use of pulldown assays to reveal histone chaperone-histone interactions, AUC, which we also use to analyze the stoichiometry of protein complexes, and histone chaperone assays to characterize putative histone chaperones in vitro functionally.

• Co-immunoprecipitation (CoIP) / pulldown

We can immunoprecipitate your protein of interest from soluble chromatin-containing fractions and then evaluate binding to core histones and association with different histone modifications by immunoblotting. We utilize recombinant bait proteins incubated in soluble fractions containing nucleosomes and purified. Similarly, we can use pulldown for histone post-translational modification binding chaperone characterization.

• Peptide pulldown

The preference of a protein for a modification can be determined by comparing the relative affinity of that protein for different modified peptides. We can use peptides immobilized on beads to pull down a protein to be tested using recombinant proteins or nuclear extracts and use immunoblotting to determine the relative recovery of the protein. This can be used to discover previously unknown histone post-translational modification binding proteins.

• Peptide microarrays

We provide an array-based method capable of simultaneously screening for interactions between a probe protein and multiple peptides. Proteins of interest are incubated on the surface of a peptide microarray, which is essentially a slide coated with the antibiotic protein streptavidin and spotted with different biotin-labeled peptides. The protein-peptide complexes can be visualized by detecting them with antibodies conjugated to fluorescent moieties and an array scanner.

Studying histone-associated chaperones is an essential component of chromatin remodeling and the dynamic regulation of epigenetic inheritance in eukaryotes. Histone molecular chaperones are involved in chromatin assembly, transcription, and repair. Lifeasible provides discovery and structural analysis of histone-associated chaperones to help you explore how to replace histones in nucleosomes and how to add modifications to histones. In-depth studies of histone molecular chaperone function can also help you better understand the mechanism of action of epigenetic regulation. Please feel free to contact us to start your project.

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For research or industrial use.

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