- 文献引用 : 6
|Application ||WB, IHC-P, E|
|Other Names||Lysine-specific demethylase 6B, 11411-, JmjC domain-containing protein 3, Jumonji domain-containing protein 3, Kdm6b, Jmjd3, Kiaa0346|
|Target/Specificity||This Mouse JMJD3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1606-1641 amino acids from the C-terminal region of mouse JMJD3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, 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||M JMJD3 Antibody (C-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. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. 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 (PubMed:21095589).|
Author : Lee JY1, Na WH2, Choi HY1, Lee KH2, Ju BG3, Yune TY4.
Neurobiol Dis. 2016 Jul 15;95:66-81. doi: 10.1016/j.nbd.2016.07.015. [Epub ahead of print]
Author : Pham D1, Yu Q, Walline CC, Muthukrishnan R, Blum JS, Kaplan MH.
J Immunol. 2013 Jul 15;191(2):902-11. doi: 10.4049/jimmunol.1203229. Epub 2013 Jun 14.
Author : Das ND, Jung KH, Choi MR, Yoon HS, Kim SH, Chai YG.
Cell Biochem Funct. 2012 Apr;30(3):224-32. doi: 10.1002/cbf.1839. Epub 2012 Jan 18.
Author : SolÃ¡ S, Xavier JM, Santos DM, Aranha MM, Morgado AL, Jepsen K, Rodrigues CM.
PLoS One. 2011 Mar 31;6(3):e18421. doi: 10.1371/journal.pone.0018421.
Author : McLaughlin-Drubin ME1, Crum CP, Münger K.
Proc Natl Acad Sci U S A. 2011 Feb 1;108(5):2130-5. doi: 10.1073/pnas.1009933108. Epub 2011 Jan 18.
Author : Das ND, Jung KH, Chai YG.
PLoS One. 2010 Mar 29;5(3):e9913. doi: 10.1371/journal.pone.0009913.
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.