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Merck
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M5820

Sigma-Aldrich

M344

≥98% (HPLC), powder

동의어(들):

4-(Dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]-benzamide, MS 344, D237, N-Hydroxy-7-(4-dimethylaminobenzoyl)-aminoheptanamide

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모든 사진(1)

About This Item

실험식(Hill 표기법):
C16H25N3O3
CAS Number:
251456-60-7
Molecular Weight:
307.39
MDL number:
MFCD03453554
UNSPSC 코드:
12352200
PubChem Substance ID:
329818022
NACRES:
NA.77

Quality Level

100

분석

≥98% (HPLC)

형태

powder

저장 조건

protect from light

색상

white to beige

solubility

DMSO: 10 mg/mL, clear

저장 온도

2-8°C

SMILES string

CN(C)c1ccc(cc1)C(=O)NCCCCCCC(=O)NO

InChI

1S/C16H25N3O3/c1-19(2)14-10-8-13(9-11-14)16(21)17-12-6-4-3-5-7-15(20)18-22/h8-11,22H,3-7,12H2,1-2H3,(H,17,21)(H,18,20)

InChI key

MXWDSZWTBOCWBK-UHFFFAOYSA-N

생화학적/생리학적 작용

M344 is a HDAC inhibitor; subtype selective for HDAC6 over HDAC1. M344 inhibits HDAC (IC50 = 100 nM) and also inhibits hyperacetylation of histone H4, terminal cell differentiation, transcription (γ-globin), and tumor cell death.

특징 및 장점

This compound is a featured product for Gene Regulation research. Click here to discover more featured Gene Regulation products. Learn more about bioactive small molecules for other areas of research at sigma.com/discover-bsm.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

시험 성적서(COA)

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R Pérez-Carro et al.
Clinical genetics, 86(2), 167-171 (2013-07-31)
Hereditary tyrosinemia type I (HT1) is a rare disease caused by a deficiency of fumarylacetoacetate hydrolase (FAH) in the tyrosine catabolic pathway, resulting mainly in hepatic alterations due to accumulation of the toxic metabolites fumarylacetoacetate, maleylacetoacetate and succinylacetone. We have
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Oncotarget, 7(6), 6727-6747 (2016-01-07)
Activator protein 1 (AP-1) is a transcriptional factor composed of the dimeric members of bZIP proteins, which are frequently deregulated in human cancer cells. In this study, we aimed to identify an oncogenic AP-1 dimer critical for the proliferation of
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It is widely assumed that decreasing transcription factor DNA-binding affinity reduces transcription initiation by diminishing occupancy of sequence-specific regulatory elements. However, in vivo transcription factors find their binding sites while confronted with a large excess of low-affinity degenerate motifs. Here, using
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Biochemistry, 54(42), 6501-6513 (2015-10-16)
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