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JMJD2A Tudor Domains (888-1023 aa) (GST-tagged), Human recombinant
A trimethylation-specific demethylase
Product Overview
Product Name: JMJD2A Tudor Domains (888-1023 aa) (GST-tagged), Human recombinant
Alternate Name/Synonyms: JHDM3A; Jumonji Domain Containing 2A; KDM4A
Gene Symbol: KDM4A
Accession #: O75164
Gene ID: 9682
Source: E. coli
Appearance: Liquid
Physical Form Description: 50 mM Tris-HCl, pH 8.0, 150 mM sodium chloride, and 20% glycerol.
Molecular Weight: 42.2 kDa (888-1023 aa, NT GST Tag)
Purity by SDS-PAGE: ≥90%
Purity by HPLC: N/A
Endotoxin Level: N/A
Biological Activity: N/A.
Reconstitution Instructions: N/A
Storage Temp.: -80°C
Shipping: Dry ice
Background Information: 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.
Amino Acid Sequence: N/A
Handling: Centrifuge the vial prior to opening
USAGE: For Research Use Only! Not For Use in Humans. |