- CITATIONS: 15
|Application ||IF, IHC-P, WB, E|
|Calculated MW||176632 Da|
|Antigen Region||1-30 aa|
|Other Names||Lysine-specific demethylase 6B, 11411-, JmjC domain-containing protein 3, Jumonji domain-containing protein 3, Lysine demethylase 6B, KDM6B, JMJD3, KIAA0346|
|Target/Specificity||This JMJD3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human JMJD3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||JMJD3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17825402, PubMed:17851529, PubMed:17713478, PubMed:18003914). Demethylates trimethylated and dimethylated H3 'Lys-27' (PubMed:17825402, PubMed:17851529, PubMed:17713478, PubMed:18003914). Plays a central role in regulation of posterior development, by regulating HOX gene expression (PubMed:17851529). Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation (PubMed:17825402). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression by acting as a link between T-box factors and the SMARCA4- containing SWI/SNF remodeling complex (By similarity).|
Provided below are standard protocols that you may find useful for product applications.
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.
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