Product nameAnti-KDM4A / JHDM3A / JMJD2A antibody - C-terminal
See all KDM4A / JHDM3A / JMJD2A primary antibodies
DescriptionRabbit polyclonal to KDM4A / JHDM3A / JMJD2A - C-terminal
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Rat, Human
Predicted to work with: Mouse, Cow
Recombinant fragment within Human KDM4A/ JHDM3A/ JMJD2A (C terminal). The exact sequence is proprietary.
Database link: O75164
- WB: Rat brain extract; HeLa whole cell and nuclear extracts.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.00
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: PBS, 20% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab228713 in the following tested applications.
|WB||1/500 - 1/3000. 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 - C-terminal (ab228713) at 1/500 dilution + Rat brain extract at 50 µg
Predicted band size: 120 kDa
5% SDS-PAGE gel.
All lanes : Anti-KDM4A / JHDM3A / JMJD2A antibody - C-terminal (ab228713) at 1/500 dilution
Lane 1 : HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell extract
Lane 2 : HeLa nuclear extract
Lysates/proteins at 30 µg per lane.
All lanes : HRP-conjugated anti-rabbit IgG
Predicted band size: 120 kDa
7.5% SDS-PAGE gel.
ab228713 has not yet been referenced specifically in any publications.