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SCP0168

Sigma-Aldrich

Histone Deacetylase Substrate

≥95% (HPLC), lyophilized

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About This Item

Fórmula empírica (notación de Hill):
C23H31N3O6
Peso molecular:
445.51
UNSPSC Code:
12352204
NACRES:
NA.32

Nombre del producto

Histone Deacetylase Substrate,

assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥85%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

BOC-Ac-Lys-AMC

Application

BOC-Ac-Lys-AMC (MAL) is used as a fluorogenic substrate for assaying both human zinc and NAD+-dependent histone deacetylases.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
LI0488

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Birgit Heltweg et al.
Methods (San Diego, Calif.), 36(4), 332-337 (2005-08-10)
Histone deacetylases are important regulators of transcription and an emerging target for anticancer drugs. We present an overview over various assay formats that include radiolabelled histones, oligopeptides, and small molecules as substrates. The advantages and disadvantages of the various formats
Birgit Heltweg et al.
Analytical biochemistry, 319(1), 42-48 (2003-07-05)
Histone deacetylases (HDACs) are involved in the regulation of transcription and their inhibitors are a promising class of new anticancer drugs. We have previously reported Boc(Ac)Lys-AMC, also termed MAL, as a fluorescent substrate for HDACs. Now we present a modification
Neetinkumar D Reddy et al.
Chemico-biological interactions, 233, 81-94 (2015-04-01)
The potential of cinnamic acid as an anti-inflammatory and anti-cancer agent has been studied previously. In our investigation, novel bio-isosters of cinnamyl sulfonamide hydroxamate were synthesized, characterized and confirmed for their structure and evaluated for cytotoxicity. Three NCEs namely, NMJ-1

Artículos

Histone Modification and Chromatin Remodeling | Epigenetics

Epigenetic modifications are thought to occur through two key interconnected processes—DNA methylation and the covalent modification of histones.

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