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Immunogen sequence: MRAGPEPQAL AGQKRGALRL LVPRLVLTVS APAEVRRRVL RPVLSWMDRE TRALADSHFR GLGVDVPGVG QAPGRVAFVS EPGAFSYADF VRGFLLPNLP CVFSSAFTQG WGSRRRWVTP AGRPDFDHLL RTYGDVVVPV ANCGVQEYNS NPKEHMTLRD YITYWKEYIQ AGYSSPRGCL YLKDWHLCRD FPVEDVFTLP VYFSSDWLNE FWDALDVDDY RFVYAGPAGS WSPFHADIFR SFSWSVNVCG RKKWLLFPPG QEEALRDRHG NLPYDVTSPA LCDTHLHPRN QLAGPPLEIT QEAGEMVFVP SGWHHQVHNL DDTISINHNW VNGFNLANMW RFLQQELCAV QEEVSEWRDS MPDWHHHCQV IMRSCSGINF EEFYHFLKVI AEKRLLVLRE AAAEDGAGLG FEQAAFDVGR ITEVLASLVA HPDFQRVDTS AFSPQPKELL QQLREAVDAA AAP; Positive Samples: 293T, HepG2, NCI-H460, BT-474, MCF7, Mouse liver, Mouse brain, Rat liver
Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe(II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36), and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9). Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: 2-oxoglutarate and iron-dependent oxygenase JMJD4; 2-oxoglutarate- and Fe(II)-dependent oxygenase; C4 lysyl hydroxylase; JmjC domain-containing protein 4; Jumonji domain-containing protein 4; Lysyl-hydroxylase JMJD4
Gene Aliases: 6430559I23; JMJD4; RGD1307186
UniProt ID: (Human) Q9H9V9, (Mouse) Q8BFT6
Entrez Gene ID: (Human) 65094, (Rat) 287359, (Mouse) 194952
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