JMJD2A Tudor Domains (888-1023 aa) (GST-tagged), Human recombinant protein
JMJD2A Tudor Domains (888-1023 aa) (GST-tagged), Human recombinant
|Calculated MW||42.2 kDa (888-1023 aa, NT GST Tag)|
|Other Names||JHDM3A; Jumonji Domain Containing 2A; KDM4A|
|Storage||-80°C; 50 mM Tris-HCl, pH 8.0, 150 mM sodium chloride, and 20% glycerol.|
firstname.lastname@example.org, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
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. Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling. The tudor domains recognize symmetric methylated arginine or methylated lysine residues. JMJD2A catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3). However, the tudor domain of this protein has been shown to bind histone H3K4me, H3K9me3, and H3K20me2/3. Like other JmjC protein hydroxylase family members, JMJD2A is an α-ketoglutarate-dependent Fe (II) oxygenase. This product contains the tandem tudor domains of JMJD2A.
Ishikawa K.,et al.DNA Res. 5:169-176(1998).
Gregory S.G.,et al.Nature 441:315-321(2006).
Gray S.G.,et al.J. Biol. Chem. 280:28507-28518(2005).
Zhang D.,et al.Mol. Cell. Biol. 25:6404-6414(2005).
Whetstine J.R.,et al.Cell 125:467-481(2006).
If you have any additional inquiries please email technical services at email@example.com.