|Other Names||Lysine-specific demethylase 3B, 11411-, JmjC domain-containing histone demethylation protein 2B, Jumonji domain-containing protein 1B, Nuclear protein 5qNCA, KDM3B, C5orf7, JHDM2B, JMJD1B, KIAA1082|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||C5orf7, JHDM2B, JMJD1B, KIAA1082|
|Function||Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity.|
|Tissue Location||Ubiquitous. Highly expressed in placenta, skeletal muscle, kidney, heart and liver|
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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.
Rose, J. Phd, et al. Mol. Med. (2010) In press :Olsen, J.V., et al. Cell 127(3):635-648(2006)Olsen, J.V., et al. Cell 127(3):635-648(2006)Yamane, K., et al. Cell 125(3):483-495(2006)Andersen, J.S., et al. Nature 433(7021):77-83(2005)
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