Active • Host: Insect cells • AA: 1-488 (full length) • Tag: C-terminal His • MW: 56.1 kDa
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HDAC2 (human, recombinant)

Item No. 36419

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Histone Deacetylase 2
Purity
≥80% estimated by SDS-PAGE
Source
Active recombinant human C-terminal His-tagged HDAC2 expressed in insect cells
Amino Acids
1-488
MW
56.1 kDa
Formulation (Request formulation change)
20 mM potassium phosphate, pH 7.6, with 100 mM sodium chloride, 1 mM DTT, and 20% glycerol
UniProt Accession №
Q92769
Shipping & Storage Information
Storage
-80°C
Shipping
Wet ice in continental US; may vary elsewhere
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    50 µg

    $520

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    Cayman Chemical
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    Product Description

    Histone deacetylase 2 (HDAC2) is a class I HDAC that catalyzes the zinc-dependent deacetylation of core histones.1,2 It is primarily localized to the nucleus and is found in all human cell lines and tissues. HDAC2 is a component of various histone deacetylation and corepressor complexes with diverse roles in chromatin manipulation and the regulation of gene expression.3 It exhibits low enzymatic activity when in isolation, which increases greatly upon its incorporation into gene expression regulatory complexes. Dysregulation of HDAC2 is associated with various diseases, including cancer, Alzheimer’s disease, stroke, and alcohol addiction.3,4,5,6 HDAC2 binds to the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (Mpro), also known as 3C-like protease (3CLpro).7 Cayman’s HDAC2 (human, recombinant) protein can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Lin, H.Y., Chen, C.S., Lin, S.P., et al. Targeting histone deacetylase in cancer therapy. Med. Res. Rev. 26(4), 397-413 (2006).

    2. Huang, L. Targeting histone deacetylases for the treatment of cancer and inflammatory diseases. J. Cell. Physiol. 209(3), 611-616 (2006).

    3. Seto, E., and Yoshida, M. Erasers of histone acetylation: The histone deacetylase enzymes. Cold Spring Harb. Perspect. Biol. 16(4), a018713 (2014).

    4. Mahady, L., Nadeem, M., Chen, K., et al. HDAC2 dysregulation in the nucleus basalis of Meynert during the progression of Alzheimer’s disease. Neuropathol. Appl. Neurobiol. 45(4), 380-397 (2019).

    5. Tang, Y., Lin, Y.-H., Ni, H.-Y., et al. Inhibiting histone deacetylase 2 (HDAC2) promotes functional recovery from stroke. J. Am. Heart Assoc. 6(10), e007236 (2017).

    6. Pandey, S.C., Kyzar, E.J., and Zhang, H. Epigenetic bases of the dark side of alcohol addiction. Neuropharmacology 122, 74-84 (2017).

    7. Gordon, D.E., Jang, G.M., Bouhaddou, M., et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 583(7816), 459-468 (2020).