Host: E. coli • AA: 1-103 (full length) • Tag: N-terminal His • MW: 13.4 kDa
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Histone H4 (human, recombinant; His-tagged)

Item No. 38257

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Purity
≥80% estimated by SDS-PAGE
Source
Recombinant human N-terminal His-tagged histone H4 expressed in E. coli
Amino Acids
1-103
MW
13.4 kDa
Formulation (Request formulation change)
A solution in water
UniProt Accession №
P62805
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    250 µg

    $259

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    Product Description

    Histone H4 is one of four core histone proteins that are involved in the organization of DNA into chromatin.1 Histones are globular proteins with unstructured N-terminal tails and are subject to a variety of post-translational modifications (PTMs), such as methylation, acetylation, phosphorylation, and citrullination, that can influence chromatin structure and regulate gene transcription.1,2 Histone H4 PTMs function as epigenetic regulators of transcription by affecting chromatin structure and enhancing transcription factor binding, as well as play a key role in the maintenance of genomic integrity.3,4 Levels of histone H4 are increased in the inferior and middle temporal gyrus in postmortem brains from patients with Alzheimer’s disease.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Wang, Y., Li, M., Stadler, S., et al. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. J. Cell Biol. 184(2), 205-213 (2009).

    2. Hyun, K., Jeon, J., Park, K., et al. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).

    3. Vettese-Dadey, M., Grant, P.A., Hebbes, T.R., et al. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J. 15(10), 2508-2518 (1996).

    4. Jørgensen, S., Schotta, G., and Sørensen, C.S. Histone H4 Lysine 20 methylation: Key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41(5), 2797-2806 (2013).

    5. Narayan, P.J., Lill, C., Faull, R., et al. Increased acetyl and total histone levels in post-mortem Alzheimer’s disease brain. Neurobiol. Dis. 74, 281-294 (2015).