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HDAC10 (human), (recombinant) (His-tag)

Highly active
BML-SE559-0050 50 µg 553.00 USD
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Deacetylates lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.

Product Details

Alternative Name:Histone deacetylase 10
MW:~71 kDa
Source:Produced in Sf9 insect cells. HDAC10 from human cDNA, transcript variant 1 (identical to GenBank accession NM_032019) is fused at the C-terminus to a His-tag. Produced in a baculovirus expression system.
UniProt ID:Q969S8
Formulation:Liquid. In 50mM TRIS, pH 8.0, containing 138mM NaCl and 10% glycerol.
Purity Detail:Partially purified by single-step affinity chromatography and gel filtration.
Biological Activity:Hydrolysis of N-ε-acetyl-lysine residues of histones.
Specific Activity:≥2U/µg. One unit is defined as the amount of enzyme that deacetylates 1 pmol/min of FLUOR DE LYS®-SIRT1 substrate (Prod. No. BML-KI177) at 37°C / 500µM.
Application Notes:Useful for studies of enzyme kinetics, modulator activity, drug discovery.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable on ice for approx. 1h. Snap freezing in liquid nitrogen is recommended if refreezing of remaining, undiluted enzyme is necessary. Freezing and storage of diluted enzyme is not recommended.
Handling:Avoid freeze/thaw cycles.
Scientific Background:HDAC10 is ubiquitously expressed in human tissues and many cell lines.  Its domain structure resembles that of its closest homolog and fellow class IIb HDAC, HDAC6, but rather than two active deacetylase domains, it has one active domain (N-terminal) and a partially duplicated, inactive, C-terminal domain. Also like HDAC6, HDAC10 is resistant to inhibition by trapoxin B, sodium butyrate and valproic acid. Inhibition of one or both of the class IIb HDACs may be a desirable goal for cancer therapy.  Inhibition or siRNA knockdown of both HDAC10 and HDAC6 causes depletion of the VEGFR1 and VEGFR2 proteins, suggesting a strategy for blocking angiogenesis via HDAC6/HDAC10 inhibition.  An HDAC10 promoter polymorphism that increases transcription is associated with increased occurence of hepatocellular carcinoma in individuals with chronic hepatitis B infections.
Regulatory Status:RUO - Research Use Only

Product Literature References

Design, Synthesis, and biological evaluation of HDAC6 inhibitors based on Cap modification strategy: X. Li, et al.; Bioorg. Chem. 125, 105874 (2022), Abstract;
Histone deacetylase 10 regulates DNA mismatch repair and may involve the deacetylation of MutS homolog 2: R. Radhakrishnan, et al.; J. Biol. Chem. 290, 22795 (2015), Abstract; Full Text
Novel analogs targeting histone deacetylase suppress aggressive thyroid cancer cell growth and induce re-differentiation: S. Jang, et al. ; Cancer Gene Ther. 22, 410 (2015), Application(s): Assay, Abstract;
Tumor-suppressor role of Notch3 in medullary thyroid carcinoma revealed by genetic and pharmacological induction: R. Jaskula-Sztul, et al.; Mol. Cancer Ther. 14, 499 (2015), Abstract; Full Text

General Literature References

Class II histone deacetylases play pivotal roles in heat shock protein 90-mediated proteasomal degradation of vascular endothelial growth factor receptors.: J. H. Park, et al.; Biochem. Biophys. Res. Commun. 368, 318 (2008), Abstract;
HDAC10 promoter polymorphism associated with development of HCC among chronic HBV patients.: B. L. Park, et al.; Biochem. Biophys. Res. Commun. 363, 776 (2007), Abstract;
Histone deacetylase is a target of valproic acid-mediated cellular differentiation: N. Gurvich, et al.; Cancer Res. 64, 1076 (2004), Abstract; Full Text
Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain.: J. J. Tong, et al.; Nucleic Acids Res. 30, 1114 (2002), Abstract; Full Text
Isolation and characterization of a novel class II histone deacetylase, HDAC10.: D. D. Fischer, et al.; J Biol. Chem. 277, 6656 (2002), Abstract; Full Text
Isolation and characterization of mammalian HDAC10, a novel histone deacetylase.: H. Y. Kao, et al; J Biol. Chem. 277, 187 (2002), Abstract; Full Text
Molecular cloning and characterization of a novel histone deacetylase HDAC10.: A. R. Guardiola & T. P. Yao; J Biol. Chem. 277, 3350 (2002), Abstract; Full Text

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