一般描述
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.
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.
生化/生理作用
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.
特点和优势
- 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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WGK
WGK 3
闪点(°F)
closed cup
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closed cup
法规信息
新产品
Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor.
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.
Structure, 12(7), 1325-1334 (2004)
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
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
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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