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VS-HSV00051 - pG-10-hH3.1; 15ug


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Expression of EGFP Fusion Proteins for the Investigation of the Histones

  • 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

In eukaryotic cell nuclei, histones pack the DNA into structural units called nucleosomes which aggregate to form chromatin. Histones are grouped in families: histones H2A, H2B, H3, and H4 are the core histones while H1 and H5 are linker histones. Histone variants are a group of proteins that adopt similar structural folds and share sequence homology with their corresponding canonical histones. The majority are variants of histone H3 or H2A. Two of each of the core histones assemble to form one octameric nucleosomal core. 147 base pairs of DNA wrap around this core particle 1.65 times in a left-handed super-helical turn. The linker histone H1 binds the nucleosome at the entry and exit sites of the linker DNA. Histones undergo posttranslational modifications that alter their interaction with DNA and nuclear proteins. The H3 and H4 histones have long tails protruding from the nucleosome, which can be covalently modified at several places. The core of the histones H2A, H2B, and H3 can also be modified. Histone modifications act in diverse biological processes such as gene regulation, DNA repair, mitosis, and meiosis. We offer expression vectors coding for human histone proteins (and their mutants) 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-hH2A1 the linker length is 20 amino acids).

Stepwise nucleosome assembly. First, two H3-H4 dimers bind and wrap the DNA. CAF-1 binds H3-H4 synthesized in the cytoplasm during S-phase, transports the heterodimer into the nucleus, and targets the complex to the replicating DNA. Two H2A-H2B dimers are then incorporated, thus establishing the mature nucleosome, called the 'octasome'.

The histone EGFP fusion proteins can be used in modern fluorescence microscopy techniques to determine
  • localization
  • binding
  • dynamics, and, when a second color is available
  • protein-protein interactions
  • protein-protein proximities
applying fluorescence methods like FRET, FRAP, FCS, RICS, FCCS, and F3H.

Please note:
For FRET analysis we suggest fusion proteins with short linker