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Merck

EPI006

Sigma-Aldrich

Histone Deacetylase 8 (HDAC8) Activity Assay Kit

100 assays in 96 well plates

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352200
NACRES:
NA.41

usage

100 assays in 96 well plates

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... HDAC8(55869)
mouse ... HDAC8(70315)

General description

HDAC8 (histone deacetylase 8) is a class I enzyme, that has 377 residues and it lies between class I and class II HDACs. This gene is located on X chromosome. It consists of a single α/β domain, in which eight parallel stranded β sheets are sandwiched between 13 α helices.
Histone deacetylases (HDACs) are a large family of enzymes that remove acetyl groups from histone proteins. Site specific histone acetylation and deacetylation have been shown to activate or repress eukaryotic gene transcription, respectively, and as a consequence, it plays a crucial role in mammalian development and disease. HDACs are involved in important biological activities, such as cell differentiation, proliferation, apoptosis, and senescence.

With Sigma′s HDAC8 Activity Assay Kit, HDAC8 present in a test sample will act with the supplied Developer, to deacetylate and then cleave the HDAC8 Substrate (R-H-K(Ac)-K(Ac)-AFC). This activity will release the quenched fluorescent group, AFC, which can be detected at Em/Ex = 380/500 nm. Trichostatin A is an HDAC inhibitor included in the kit to verify HDAC8 activity. The kit provides a rapid, simple, sensitive, and reliable test. It is suitable for either individual tests or high throughput assays, from nuclear extracts, purified, or immunoprecipitated HDAC8, and from native, recombinant, or genetically modified HDAC8.

Biochem/physiol Actions

HDAC8 (histone deacetylase 8), with the help of PKA (cyclic AMP-dependent protein kinase A) plays a major role in confirming the acetylation state of histones. This protein may also plays an important role in acute myeloid leukemia (AML). Suppression of HDAC8 by RNA interference stops the growth of lung, colon, and cervical cancer cell lines.

Features and Benefits

  • Simple, sensitive, and reliable assay
  • Utilizes fluorometric methods
  • Sample type: cell and tissue lysates, plasma and serum, other biological fluids
  • Species reactivity: mammalian
  • Suitable for individual tests or high throughput assays and kinetic studies
  • Suitable for high throughput measurement of HDAC8 activity in purified, immunoprecipitated, and recombinant or genetically modified HDAC8 samples
  • Convenient 96-well microplate format

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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

188.6 °F - closed cup

flash_point_c

87 °C - closed cup


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Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor.
Vannini A, et al.
Proceedings of the National Academy of Sciences of the USA, 101(42), 15064-15069 (2004)
Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases.
Somoza JR, et al.
Structure, 12(7), 1325-1334 (2004)
Bihua Bie et al.
Nature neuroscience, 17(2), 223-231 (2014-01-21)
Amyloid-induced microglial activation and neuroinflammation impair central synapses and memory function, although the mechanism remains unclear. Neuroligin 1 (NLGN1), a postsynaptic protein found in central excitatory synapses, governs excitatory synaptic efficacy and plasticity in the brain. Here we found, in
Yong Wang et al.
Circulation research, 114(6), 957-965 (2014-01-31)
Our previous study has shown that yes-associated protein (YAP) plays a crucial role in the phenotypic modulation of vascular smooth muscle cells (SMCs) in response to arterial injury. However, the role of YAP in vascular SMC development is unknown. The
Ji Heon Noh et al.
Cancer research, 74(6), 1728-1738 (2014-01-23)
Aberrant regulation of histone deacetylase 2 (HDAC2) contributes to malignant progression in various cancers, but the underlying mechanism leading to the activation of oncogenic HDAC2 remains unknown. In this study, we show that HDAC2 expression is upregulated in a large

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