JMJD2A tudor domains (human recombinant)【科瑞奥博】

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JMJD2A tudor domains (human recombinant)

货号： 14134-100ug 基本售价： 3990.0 元规格： 100 ug

产品信息

概述
货号	14134-100ug
描述	*Key Features* Cayman’s JMJD2A Tudor Domains TR-FRET Assay Kit (Item No. 700960) was developed using JMJD2A tudor domains (human recombinant) protein. Bulk sizes available upon request Tudor domains are small protein structural motifs of about ~50 amino acids related to the “royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains.^1,2 Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are invloved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling.³ The tudor domains recognize symmetric methylated arginine or methylated lysine residues.^4,5,6,7 JMJD2A catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3).⁸ However, the tudor domain of this protein has been shown to bind histone H3K4me, H3K9me3, and H3K20me2/3.⁴ Like other JmjC protein hydroxylase family members, JMJD2A is an α-ketoglutarate-dependent Fe (II) oxygenase.⁸ This product contains the tandem tudor domains of JMJD2A.
别名	JHDM3A;Jumonji Domain Containing 2A;KDM4A;

性能
供应商	Cayman
应用文献
1.Maurer-Stroh, S.,Dickens, N.J.,Hughes-Davies, L., et al. The Tudor domain Royal Family: Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends in Biochemical Sciences 28(2), 69-74 (2003). 2.Lasko, P. Tudor domain. Current Biology 20(16), R666-R667 (2010). 3.Chen, C.,Nott, T.J.,Jin, J., et al. Deciphering arginine methylation: Tudor tells the tale. Nature Reviews.Molecular Cell Biology 12(10), 629-642 (2011). 4.Kim, J.,Daniel, J.,Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO reports 7(4), 397-403 (2006). 5.Huang, Y.,Fang, J.,Bedford, M.T., et al. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312, 748-751 (2006). 6.Lee, J.,Thompson, J.R.,Botuyan, M.V., et al. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nature Structural & Molecular Biology 15(1), 109-111 (2008). 7.Sprangers, R.,Groves, M.R.,Sinning, I., et al. High-resolution X-ray and NMR structures of the SMN tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues. Journal of Molecular Biology 327(2), 507-520 (2003). 8.Couture, J.F.,Collazo, E.,Ortiz-Tello, P.A., et al. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature Structural & Molecular Biology 14(8), 689-695 (2007).
运输条件	Dry ice in continental US; may vary elsewhere
存放说明	-80
纯度	≥90% estimated by SDS-PAGE
稳定性	≥ 6 months

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