Applications
WB;IHC;IF;ELISA
Antibody type
Monoclonal antibodies
Protein name
Lysine-specific demethylase 4A
Immunogen
Purified recombinant fragment of human JMJD2A expressed in E. Coli.
Specificity
JMJD2A Monoclonal Antibody detects endogenous levels of JMJD2A protein.
Constitute
Ascitic fluid containing 0.03% sodium azide,0.5% BSA, 50%glycerol.
Dilution rate
Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/200 - 1/1000. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/10000. Not yet tested in other applications.
Purification process
Affinity purification
Other name
KDM4A; JHDM3A; JMJD2; JMJD2A; KIAA0677; Lysine-specific demethylase 4A; JmjC domain-containing histone demethylation protein 3A; Jumonji domain-containing protein 2A
Background
This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor. [provided by RefSeq, Apr 2009],
Function
cofactor:Binds 1 Fe(2+) ion per subunit.,domain:The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue. 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' 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 able to bind trimethylated histone H3 'Lys-4', trimethylated histone H3 'Lys-9', di- and trimethylated H4 'Lys-20'.,function:Histone 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' r
