Active • Host: Insect cells • AA: 518-952 • Tag: N-terminal GST • MW: 78 kDa
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HDAC7 (human, recombinant)

Item No. 42084

Product Insert (PDF)
Technical Information
Synonyms
  • Histone Deacetylase 7
Purity
≥56% estimated by SDS-PAGE
Source
Active recombinant human N-terminal GST-tagged HDAC7 expressed in insect cells
Amino Acids
518-952
MW
78 kDa
Storage Buffer
40 mM Tris-HCl, pH 8.0, 250 mM sodium chloride, and 20% glycerol
UniProt Accession №
Q8WUI4
Shipping & Storage Information
Storage
-80°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Histone deacetylase 7 (HDAC7) is a zinc-dependent metalloenzyme and class IIa HDAC.1 It is composed of an N-terminal regulatory domain, which contains a myocyte-specific enhancer factor 2 (MEF2) binding site, three 14-3-3 binding sites, and a nuclear localization signal, a catalytic domain, and a C-terminal domain that contains a nuclear export signal.1 HDAC7 shuttles between the cytoplasm, mitochondria, and nucleus and is expressed in the heart, placenta, pancreas, lungs, and skeletal muscle.2,3 It acts as a transcriptional corepressor and has many binding partners, including MEF2, nuclear receptor co-repressor (NCOR), and hypoxia-inducible factor-1α (HIF-1α), and its enzymatic activity is dependent on association with HDAC3.1,2 HDAC7 is involved in immunity, angiogenesis, embryonic development, muscle cell differentiation, and apoptosis.4,5,3 Knockdown of HDAC7 inhibits sphere formation of breast cancer stem cells (CSCs) in vitro.6 Hdac7-/- is embryonic lethal and induces hemorrhages, pericardial effusion, and enlarged dorsal aortae in mice.7 Expression of HDAC7 is increased in patients with various cancers and is associated with poor prognosis.4 Cayman's HDAC7 (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. Yang, X.J., and Grégoire, S. Class II histone deacetylases: From sequence to function, regulation, and clinical implication. Mol. Cell. Biol. 25(8), 2873-2884 (2005).

    2. Fischle, W., Dequiedt, F., Fillion, M., et alHuman HDAC7 histone deacetylase activity is associated with HDAC3 in vivo. The Journal of Biological Chemisty 276(38), 35826-35835 (2001).

    3. Bakin, R.E., and Jung, M.O. Cytoplasmic sequestration of HDAC7 from mitochondrial and nuclear compartments upon initiation of apoptosis. The Journal of Biological Chemisty 279(49), 51218-51225 (2004).

    4. Liu, C., Zheng, D., Pu, X., et alHDAC7: A promising target in cancer. Front. Oncol. 14, 1327933 (2024).

    5. de Ruijter, A.J., van Gennip, A.H., Caron, H.N., et alHistone deacetylases (HDACs): Characterization of the classical HDAC family. Biochem J. 370(Pt 3), 737-749 (2003).

    6. Witt, A.E., Lee, C.-W., Lee, T.I., et alIdentification of a cancer stem cell-specific function for the histone deacetylases, HDAC1 and HDAC7, in breast and ovarian cancer. Oncogene 36(12), 1707-1720 (2017).

    7. Chang, S., Young, B.D., Li, S., et alHistone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Cell 126(2), 321-334 (2006).