Vectors for Expression of Human Chaperone Fusion Proteins
Expression of EGFP Fusion Proteins for the Investigation of the Chaperones
Chaperones involved in H3 accumulation and incorporation in telomeric, centric and pericentric chromatin
- Ready-to-use vectors for live cell imaging
- Large selection of genes
- Sequence-documented vectors
- Applications include localization, binding, and protein-protein interaction studies
- Experimentally approved
- Molecular chaperones are proteins that assist the non-covalent folding or unfolding, and the assembly or disassembly of other macromolecular structures. Histone chaperones are a group of proteins that bind histones and regulate nucleosome assembly. In general, histone chaperones can be classified as either H3-H4 or H2A-H2B chaperones based on their preferential histone binding. In addition to canonical histones, a unique histone chaperone may exist for each histone variant (e.g., DAXX and HIRA for H3.3, CAF1 for H3.1). Histone chaperones participate in distinct steps of nucleosome assembly. Some histone chaperones, such as Nap1, help to shuttle newly synthesized histones from the cytoplasm to the nucleus, while others, such as NASP, act as histone reservoirs and regulate histone supply, or, such as RbAp46 and Asf1, directly regulate the enzymatic activity of histone-modifying enzymes. Further histone chaperones are directly involved in the deposition of histones onto DNA for nucleosome assembly. MoBiTec offers expression vectors coding for human chaperone proteins in fusion with EGFP. Most of the fusion proteins can be expressed either with N- or C-terminal EGFP-tag. The cipher in the vector name indicates the linker length of the fusion proteins (e.g., for vector pG-20-hCaf1B the linker length is 20 amino acids).
- The chaperone EGFP fusion proteins can be used in modern fluorescence microscopy techniques to determine
- dynamics, and, when a second color is available,
- protein-protein interactions and
- protein-protein proximities
- For FRET analysis we suggest fusion proteins with short linker.
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