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.
Category
Antibodies
Product Group
Polyclonal Antibodies
Application
ELISA, WB
Host
Rabbit
Species reactivity
Human
Formulation
In 1X PBS, pH 7.4, with 0.09% sodium azide
Immunogen
A portion of amino acids 1-30 from the human protein was used as the immunogen for this JMJD4 antibody.
Synonyms
2-oxoglutarate- and Fe(II)-dependent oxygenase; 2-oxoglutarate and iron-dependent oxygenase JMJD4; C4 lysyl hydroxylase; jmjC domain-containing protein 4; jumonji domain-containing protein 4; lysyl-hydroxylase JMJD4
