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Cat. Number
066071211204376
Chemical Name
HDAC Cell-Based Activity Assay Kit
References
Synonyms
  • Histone Deacetylase Cell-Based Activity Assay Kit
Stability 6 months
Storage -80°C
Shipping Dry ice in continental US; may vary elsewhere

Background Reading

Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389 349-352 (1997 Sep 25).

Strahl, B.D., and Allis, D. The language of covalent histone modifications. Nature 403 41-45 (2000 Jan 6).

Cheung, W.L., Briggs, D.B., and Allis, C.D. Acetylation and chromosomal functions. Curr Opin Cell Biol 12 326-333 (2000 Jan 1).

Suenaga, M., Soda, H., Oka, M., et al. Histone deacetylase inhibitors suppress telomerase reverse transcriptase mRNA expression in prostate cancer cells. Int J Cancer 97 621-625 (2002 Jan 1).

Johnstone, R.W. Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nat Rev Drug Discov 1 287-299 (2002).

Kwon, H.J., Kim, M.S., Kim, M.J., et al. Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int J Cancer 97 290-296 (2002 Jan 1).

Show all 6 Hide all but first 3
600150-96well
HDAC Assay Buffer (10X) 1 ea
HDAC Trichostatin A 1 ea
HDAC Deacetylated Standard 1 ea
HDAC Developer 1 ea
HDAC1 Positive Control 1 ea
96-Well Clear Bottom Black Culture Solid Plate
Nonidet P-40 Assay Reagent (10%) 0.5 mL
Cell-Based Assay HDAC Substrate 1 ea
Size Global Purchasing
96 wells  

Description

Nucleosomes, which fold chromosomal DNA, contain two molecules each of the core histones H2A, H2B, H3, and H4. Almost two turns of DNA are wrapped around this octameric core, which represses transcription.1 The histone amino termini extend from the core, where they can be modified post-translationally by acetylation, phosphorylation, ubiquitination, and methylation, affecting their charge and function. Acetylation of the ε-amino groups of specific histone lysines is catalyzed by histone acetyltransferases (HATs) and correlates with an open chromatin structure and gene activation. Histone deacetylases (HDACs) catalyze the hydrolytic removal of acetyl groups from histone lysine residues and correlates with chromatin condensation and transcriptional repression.2,3 Therefore, HDAC inhibition results in transcriptional activation through the conformational relaxation of DNA. Changes in the transcription of key genes has linked HDAC inhibitors to blocking angiogenesis and cell cycling, and promoting apoptosis and differentiation. By targeting these key components of tumor proliferation, HDAC inhibitors are currently being explored as potential anticancer agents.4,5,6 Cayman’s HDAC Cell-Based Assay Kit provides an easy tool for studying HDAC activity modulators in whole cells. By using a cell-permeable HDAC substrate, the activity of various protein lysine-specific deacetylases including HDAC1-containing complexes can be measured in intact cells in a simple and homogenous manner. The fluorescence of the deacetylated reaction product can be analyzed using a plate reader or a fluorometer with excitation wavelengths of 340-360 nm and emission wavelengths of 440-465 nm. An HDAC inhibitor, trichostatin A (TSA), is included for checking specificity of the HDAC reaction. This assay parallels Cayman’s HDAC Activity Assay Kit (Catalog No. 10011563), which uses a nuclear extract rather than whole cells for the assay. Together, both assays will help to identify whether an inhibitor/activator has a direct effect on the enzyme.

1 Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389 349-352 (1997 Sep 25).

2 Strahl, B.D., and Allis, D. The language of covalent histone modifications. Nature 403 41-45 (2000 Jan 6).

3 Cheung, W.L., Briggs, D.B., and Allis, C.D. Acetylation and chromosomal functions. Curr Opin Cell Biol 12 326-333 (2000 Jan 1).

4 Kwon, H.J., Kim, M.S., Kim, M.J., et al. Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int J Cancer 97 290-296 (2002 Jan 1).

5 Suenaga, M., Soda, H., Oka, M., et al. Histone deacetylase inhibitors suppress telomerase reverse transcriptase mRNA expression in prostate cancer cells. Int J Cancer 97 621-625 (2002 Jan 1).

6 Johnstone, R.W. Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nat Rev Drug Discov 1 287-299 (2002).

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