Histone N(ϵ)-methyl lysine demethylases are important in epigenetic regulation. JMJD2E (KDM4E) also known as Lysine-specific demethylase 4E, histone lysine demethylase 4E, or KDM4D-like protein, and encoded by the gene KDM4E/KDM4DL, is a member of the large Fe(II)/2-oxoglutarate- dependent family of human histone demethylases. JMJD2E (KDM4E) is a histone demethylase that specifically demethylates ′Lys-9′ of histone H3, thereby playing a central role in histone code. The KDM4 family also includes KDM4A, KDM4B, KDM4C, and KDM4D. These are also referred to as JMDM3A/JMJD2A, JMDM3B/JMJD2B, JMDM3C/JMJD2C, and JMDM3D/JMJD2D, respectively. Steady-state assays showed that KDM4E has a graded response to O2 over a physiologically relevant range of O2 concentrations, with activity level being dependent upon the methylation status of the target protein, and research with JMJD2E(KDM4E) may indicate the potential for histone demethylase activity to be regulated by oxygen availability.
Immunogen
Linear peptide corresponding to JMJD2E/KDM4E.
Application
Detect JMJD2E/KDM4E using this Anti-JMJD2E/KDM4E antibody validated for use in western blotting.
Quality
Evaluated by Western Blotting in PC-12 cell lysate.
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected JMJD2E/KDM4E in 10 µg of PC-12 cell lysate.
Target description
~65 kDa observed
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
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Hypoxia is a physiological stress that frequently occurs in solid tissues. Autophagy, a ubiquitous degradation/recycling system in eukaryotic cells, renders cells tolerant to multiple stressors. However, the mechanisms underlying autophagy initiation upon hypoxia remains unclear. Here we show that protein
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