Histone chaperones are a class of proteins with roles in chromatin remodelling, a process essential for regulating gene expression, DNA replication, repair, and genome maintenance. These proteins facilitate the dynamic exchange of histones (the proteins around which DNA is wrapped to form nucleosomes) and the assembly/disassembly of nucleosomes, contributing to the structural and functional plasticity of chromatin. They include such proteins as: 1) Nucleosome Assembly Proteins. Chaperones primarily involved in the assembly of nucleosomes during DNA replication or repair and include CAF-1 (Chromatin Assembly Factor 1) and HIRA (Histone Regulator A); 2) Histone H3-H4 Chaperones. Histone chaperones that specifically interact with histone H3-H4 dimers and are crucial for nucleosome formation. They include Asf1 (Anti-silencing Function 1), Rtt106, and HIR (Histone Regulator) complex subunits; 3) Histone H2A-H2B Chaperones. These chaperones interact with histone H2A-H2B dimers and assist in their deposition onto DNA. Examples include NAP1 (Nucleosome Assembly Protein 1) and FACT (Facilitates Chromatin Transcription) complex; 4) Heterodimeric Chaperones. These chaperones function as heterodimers, with each subunit binding to specific histone dimers. An example is the CAF-1 complex, which consists of p150 and p60 subunits; 5) ATP-Dependent Chromatin Remodellers. Some ATP-dependent chromatin remodellers, such as SWI/SNF complexes, can also function as histone chaperones by removing or repositioning histones during nucleosome remodelling, with SWI/SNF complexes and INO80 complexes being examples; 6) Histone Variants Chaperones. These chaperones are involved in the incorporation of histone variants (non-canonical histones) into chromatin. Histone variants can have specialized functions. Examples include H3.3-H4 chaperones like DAXX (Death Domain-Associated Protein) and ATRX (Alpha Thalassemia/Mental Retardation Syndrome X-Linked). In general, histone chaperones are primarily involved in the deposition and removal of histones onto or from DNA. For example, during DNA replication, they help load newly synthesized histones onto the newly replicated DNA forming nucleosomes. Conversely, after DNA repair or transcription, they assist in the removal of histones, facilitating access to the DNA. Histone chaperones aid in the assembly of nucleosomes by guiding histones to specific DNA sequences and facilitating their correct positioning. Conversely, they promote nucleosome disassembly by extracting histones from DNA, allowing for transient exposure of DNA during processes like transcription or DNA repair. Histone chaperones also play a critical role in histone exchange, which involves swapping one histone variant for another. This process can alter chromatin structure and gene expression patterns. For example, the chaperone complex responsible for depositing H2A.Z-H2B dimers onto DNA is known to include several proteins, such as INO80, SWR1 (also called SRCAP), and the H2A.Z-H2B dimer itself. This complex facilitates the exchange of canonical H2A-H2B dimers with H2A.Z-H2B dimers, influencing nucleosome stability and gene regulation. By loading or unloading specific histone variants or post-translationally modified histones, they also help determine whether a chromatin region is transcriptionally active (euchromatin) or repressed (heterochromatin). Some histone chaperones, such as ATRX/DAXX, utilize ATP-dependent chromatin remodelling complexes to facilitate histone exchange. These complexes use energy from ATP hydrolysis to disrupt histone-DNA interactions and exchange histones, leading to nucleosome remodelling. We provide a large product range of research reagents for investigating histone chaperones, including Daxx antibodies, ASF1A antibodies, and SET antibodies. Explore our full histone chaperones product range below and discover more, for less.