Product nameAnti-KDM4A / JHDM3A / JMJD2A antibody
See all KDM4A / JHDM3A / JMJD2A primary antibodies
DescriptionRabbit polyclonal to KDM4A / JHDM3A / JMJD2A
Tested applicationsSuitable for: ICC/IF, IP, ChIP, WBmore details
Species reactivityReacts with: Human
Predicted to work with: Rat
Recombinant fragment, corresponding to amino acids 592-720 of Human JMJD2A
- HeLa cell nuclear lysate.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
ChIP Related Products
Our Abpromise guarantee covers the use of ab24545 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||Use at an assay dependent concentration.|
|IP||Use at an assay dependent dilution.|
|ChIP||Use at an assay dependent dilution.|
|WB||1/2000. Detects a band of approximately 130 kDa (predicted molecular weight: 120 kDa).|
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
- JHDM3A antibody
- JmjC domain containing histone demethylation protein 3A antibody
- JmjC domain-containing histone demethylation protein 3A antibody
Anti-KDM4A / JHDM3A / JMJD2A antibody (ab24545) at 1/2000 dilution + HeLa nuclear extract
Predicted band size: 120 kDa
Observed band size: 130 kDa why is the actual band size different from the predicted?
This product has been referenced in:
- Dobrynin G et al. KDM4A regulates HIF-1 levels through H3K9me3. Sci Rep 7:11094 (2017). Read more (PubMed: 28894274) »
- Garcia J & Lizcano F KDM4C Activity Modulates Cell Proliferation and Chromosome Segregation in Triple-Negative Breast Cancer. Breast Cancer (Auckl) 10:169-175 (2016). ICC/IF ; Human . Read more (PubMed: 27840577) »