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ITM0389

ITM0389
  • Catalog: ITM0389
  • Gene/Protein: KDM4A
  • Product Description: Immunotag™ JMJD2A Monoclonal Antibody
504.0000
Price in reward points: 504

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Immunotag™ JMJD2A Monoclonal Antibody
Antibody Specification
Datasheet
Target Protein JMJD2A
Clonality Monoclonal
Storage/Stability -20°C/1 year
Application WB,IHC-p,IF,ELISA
Recommended Dilution 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.
Concentration 1 mg/ml
Reactive Species Human
Host Species Mouse
Immunogen Purified recombinant fragment of human JMJD2A expressed in E. Coli.
Specificity JMJD2A Monoclonal Antibody detects endogenous levels of JMJD2A protein.
Purification Affinity purification
Form Ascitic fluid containing 0.03% sodium azide.
Gene Name KDM4A
Accession No. O75164 Q8BW72
Alternate Names KDM4A; JHDM3A; JMJD2; JMJD2A; KIAA0677; Lysine-specific demethylase 4A; JmjC domain-containing histone demethylation protein 3A; Jumonji domain-containing protein 2A
Description lysine demethylase 4A(KDM4A) Homo sapiens 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],
Protein Expression Brain,Placenta,T-cell,
Subcellular Localization nucleus,nucleoplasm,pericentric heterochromatin,nucleolus,cytoplasm,
Protein 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' 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.,similarity:Belongs to the JHDM3 histone demethylase family.,similarity:Contains 1 JmjC domain.,similarity:Contains 1 JmjN domain.,similarity:Contains 2 PHD-type zinc fingers.,similarity:Contains 2 Tudor domains.,subunit:Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein.,tissue specificity:Ubiquitous.,
Usage For Research Use Only! Not for diagnostic or therapeutic procedures.
Material Safety Data Sheet
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