SML3395
KDM5-C70
≥95% (HPLC)
同義詞:
C 70, C-70, C70, Ethyl 2-(((2-((2-(dimethylamino)ethyl)ethylamino)-2-oxoethyl)amino)methyl)-4-pyridinecarboxylate, Ethyl 2-(((2-((2-(dimethylamino)ethyl)ethylamino)-2-oxoethyl)amino)methyl)isonicotinate, KDM5-C49 ethyl ester, KDOAM-20 ethyl ester, KDOAM-21, KDOAM20 ethyl ester, KDOAM21
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About This Item
推薦產品
品質等級
化驗
≥95% (HPLC)
形狀
oil
顏色
, Light yellow to very dark red-bown
儲存溫度
-10 to -25°C
SMILES 字串
CN(CCN(C(CNCC1=CC(C(OCC)=O)=CC=N1)=O)CC)C
生化／生理作用
KDM5-C70 (KDOAM-21) corresponds to the ethyl ester precursor of a selective αKG-competitive KDM5 histone demethylase inhibitor KDM5-C49 (KDOAM-21; KDM5A/B/C/D Ki = 2/1/6.1/3.4 nM vs. KDM4C/6B/3A/2A Ki = 0.51/4.55/2.59/4.4 μM; KDM5A/B/C/D IC50 = 1.1/0.8/3.2/2.7 μM by FDH assay with [αKG] = 1 mM & [E]/[S] = 0.5/15 μM; KDM5A/B/C IC50 = 25/30/59 nM by alphaLISA with [αKG] = 25 μM & [E]/[S] = 10/100 nM). KDM5-C70 treatment selectively upregulates cellular histone H3 trimethylation on Lys4 (H3K4me3), but not on Lys9/7/36 (5 μM, 3d), and inhibits KDM5-dependent cancer growth (by 85%/MCF7/11d, 97%/BT474/24d, and 70%/ZR-75-1/24d; 5 μM).
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號，寫有 ‘Lot’或‘Batch’.。
Structural Basis for KDM5A Histone Lysine Demethylase Inhibition by Diverse Compounds
Cell Chemical Biology, 23(7), 769-781 (2016)
Lauren P Blair et al.
Science advances, 2(11), e1501662-e1501662 (2017-02-01)
The complexity by which cells regulate gene and protein expression is multifaceted and intricate. Regulation of 3' untranslated region (UTR) processing of mRNA has been shown to play a critical role in development and disease. However, the process by which
Anthony Tumber et al.
Cell chemical biology, 24(3), 371-380 (2017-03-07)
Methylation of lysine residues on histone tail is a dynamic epigenetic modification that plays a key role in chromatin structure and gene regulation. Members of the KDM5 (also known as JARID1) sub-family are 2-oxoglutarate (2-OG) and Fe2+-dependent oxygenases acting as
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