Product nameRecombinant Human KDM4A / JHDM3A / JMJD2A protein
See all KDM4A / JHDM3A / JMJD2A proteins and peptides
Protein lengthProtein fragment
SourceBaculovirus infected Sf9 cells
Amino Acid Sequence
Molecular weight150 kDa including tags
Amino acids1 to 886
Our Abpromise guarantee covers the use of ab125541 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity> 90 % Densitometry.
Purity was determined to be >90% by densitometry.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.002% PMSF, 0.004% DTT, 0.79% Tris HCl, 0.003% EDTA, 25% Glycerol, 0.88% Sodium chloride
- JmjC domain containing histone demethylation protein 3A
- JmjC domain-containing histone demethylation protein 3A
FunctionHistone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.
Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.
Sequence similaritiesBelongs to the JHDM3 histone demethylase family.
Contains 1 C2HC pre-PHD-type zinc finger.
Contains 1 JmjC domain.
Contains 1 JmjN domain.
Contains 2 PHD-type zinc fingers.
Contains 2 Tudor domains.
DomainThe 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1.
modificationsUbiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited.
- Information by UniProt
ab125541 has not yet been referenced specifically in any publications.