Recombinant Human KDM4A / JHDM3A / JMJD2A protein (GST tag N-Terminus)
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- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human KDM4A / JHDM3A / JMJD2A protein (GST tag N-Terminus) (AB125541)
SDS-PAGE analysis of ab125541.
Reactivity data
Sequence info
Properties and storage information
Form
Purification technique
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
General info
Function
Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed : 16603238, PubMed : 26741168, PubMed : 21768309). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20' (PubMed : 16603238, PubMed : 26741168, PubMed : 21768309). Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues (PubMed : 16603238, PubMed : 26741168, PubMed : 21768309). Demethylation of Lys residue generates formaldehyde and succinate (PubMed : 16603238). Also able to demethylate histone H1-4 methylated at 'Lys-26' (H1.4K26me1, H1.4K26me2 and H1.4K26me3) (PubMed : 19144645, PubMed : 30156264). Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively (PubMed : 16024779).. 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 similarities
Belongs to the JHDM3 histone demethylase family.
Post-translational modifications
(Microbial infection) SUMOylated by human herpesvirus 8 E3 SUMO-protein ligase K-bZIP/K8 at Lys-471; thereby modulating the chromatin binding and histone demethylase activity of KDM4A.. Ubiquitinated 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. Also ubiquitinated by the SCF(FBXO22) complex; leading to proteasomal degradation (PubMed:21768309).
Target data
Alternative Names
Product promise
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