Innovative Tools for Molecular and Cell Biology

Innovative Tools for Molecular and Cell Biology


Vectors for Expression of Human Histone Fusion Proteins

Expression of EGFP Fusion Proteins for the Investigation of the Histones

Vector map of pG-20-hH2A1

Vector map of pG-20-hH2A1

Stepwise nucleosome assembly

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'.


  • 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 post-translational 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. MoBiTec offers 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).


  • The histone EGFP fusion proteins can be used in modern fluorescence microscopy techniques to determine
    1. localization,
    2. binding,
    3. dynamics, and, when a second color is available,
    4. protein-protein interactions and
    5. 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.


  • For shipping and storage information please click on Order#.


Order# Description Amount Price Data Sheet
VS-HSV00001 pG-20-hH2A.1 15 ug 453,00 PDF
VS-HSV00002 phH2A.1-15-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00003 pG-20-hH2ABbd 15 ug 453,00 PDF
VS-HSV00004 phH2ABbd-15-G 15 ug 453,00 PDF
VS-HSV00005 pG-20-hH2AX 15 ug 453,00 PDF
VS-HSV00006 phH2AX-15-G 15 ug 453,00 PDF
VS-HSV00007 pG-20-hH2AZ 15 ug 453,00 PDF
VS-HSV00008 phH2AZ-15-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00015 pG-20-hH2B1B 15 ug 453,00 PDF
VS-HSV00016 phH2B1B-15-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00051 pG-10-hH3.1 15 ug 453,00 PDF
VS-HSV00052 phH3.1-6-G 15 ug 453,00 PDF
VS-HSV00053 pG-14-hH3.1(C97A) 15 ug 453,00 PDF
VS-HSV00054 phH3.1(C97A)-15-G 15 ug 453,00 PDF
VS-HSV00055 pG-14-hH3.1(C97D) 15 ug 453,00 PDF
VS-HSV00056 phH3.1(C97D)-15-G 15 ug 453,00 PDF
VS-HSV00057 pG-14-hH3.1(C111A) 15 ug 453,00 PDF
VS-HSV00058 phH3.1(C111A)-15-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00101 pG-10-hH3.2 15 ug 453,00 PDF
VS-HSV00102 phH3.2-18-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00151 pG-10-hH3.3 15 ug 453,00 PDF
VS-HSV00153 pG-20-hH3.3(S31A) 15 ug 453,00 PDF
VS-HSV00154 phH3.3(S31A)-15-G 15 ug 453,00 PDF
VS-HSV00155 pG-20-hH3.3(G90M) 15 ug 453,00 PDF
VS-HSV00156 phH3.3(G90M)-15-G 15 ug 453,00 PDF


Order# Description Amount Price Data Sheet
VS-HSV00201 pG-20-hH4 15 ug 453,00 PDF
VS-HSV00202 phH4-15-G 15 ug 453,00 PDF
  • All prices are in EURO excl. VAT and shipping. For further pricing and order information please ask your local distributor.


  • Hitoshi K., Horikoshi N., Tachiwana H., and Kagawa W. (2013): Current progress on structural studies of nucleosomes containing histone H3 variants. Current Opinion in Structural Biology, 2013 Feb;23:109–115. Pubmed
  • Bönisch C., & Hake S.B. (2012): Histone H2A variants in nucleosomes and chromatin: more or less stable? Nucleic Acids Research, 2012 Nov;40(21):10719-41. Pubmed
  • Talbert B. P. and Henikoff S. (2010): Histone variants — Ancient Wrap Artists Of The Epigenome. Nature Reviews | Molecular cell Biology 2010 Apr;11(4):264-75. Pubmed
  • Talbert P. B., Ahmad K., Almouzni G., Ausió J., Berger F., Bhalla P.L., Bonner W.M., Cande W.Z., Chadwick B.P., Chan S.W.L., Cross G.A.M., Cui L., Dimitrov S.I., Doenecke D., Eirin-López J.M., Gorovsky M.A., Hake S.B., Hamkalo B.A., Holec S., Jacobsen S.E., Kamieniarz K., Khochbin S., Ladurner A.G., Landsman D., Latham J.A., Loppin B., Malik H.S, Marzluff W.F., Pehrson J.R., Postberg J., Schneider R., Singh M.B., Smith M.M., Thompson E., Torres-Padilla M.E., Tremethick D.J., Turner B.M., Waterborg J.H., Wollmann H., Yelagandula R., Zhu B., & Henikoff S. (2012): A unified phylogeny-based nomenclature for histone variants. Epigenetics & Chromatin 2012 Jun 21;5:7 Pubmed