Jumonji domain-containing protein 2D
Jumonji, AT-rich interactive domain 1C (JARID1C) protein belongs to the highly conserved ARID protein family, which is involved in chromatin remodeling and transcriptional regulation during cell growth, differentiation, and development. In human this gene plays an important role in normal brain development. the bioinformatic prediction indicated several conserved domains incudind an ARID domain, a JmjC domain a C5HC2 zinc finger domain and a JmJ domain. The epigenetic information encoded as methylated CpG di-nucleotides to the transcriptional machinery is transferred by a multifunction methylated DNA binding protein called Methylated CpG biding protein 2.
Jumonji domain containing 2D protein (Jmj2D) is a histone demethylase that specifically demethylates’Lys-9’ of histone H3, thereby playing a central role in histone code. Jmj2D does not demethylate histone H3 at’Lys-4’, H3 at’Lys-27’,H3 at ’Lys-36’ nor H4 at ’Lys-20’. Jmj2D demethylates both di- and trimethylated H3 ’Lys-9’ residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Differential expression of various genes has been studied in esophageal squamous cell carcinomas (ESCs) using genomic hybridization studies. Frequent amplification of DNA copy number has been reported at chromosome 9p23-24 in ESCs that is rich in oncogenes and other tumor-associated genes. One of the novel gene over-expressed in ESCs was cloned and designated as GASC1 or JmjC. The protein contains 2 PD-finger motifs and a P domain. The PHD domains are characteristics of nuclear proteins that participate in chromatin-mediated transcriptional regulation and are present in number of oncogenes (1). Jumonji domain containing protein 2D is a amino acid protein abundantly expressed in brain in gonads suggesting its role in brain and gonads functions. Jumonj3C is a histone demethylase and it demethylates Lys-9 and Lys-36 residues on histone H3 and thus play an important and central role n histone code. Interesting ly, the Jumonji3C does not demethylates histone H3 at position Lys-4, H3 lys-27 nor does it catalyze H4 Lys-20. Jmj3C demethylates trimethylated H3 Lys-9 and Lys-36 residues while it has no activity on mono and dimethylated residues. The enzymatic demethylation of lysine residues generated formaldehyde and succinate. The enzyme also binds to 1 mole of iron as a cofactor, JmjC domain belongs to the cupin susperfamily that posses protein hydroxylases that catalyze novel histone modifications (2). Jmj3C protein also contains 2 Tudor domains that recognizes and binds methylated histones, the double Tudor domain has in terdigitated structure and an unusual fold that is required for its ability to bind methylated histones by tails.
The Jmj3C-selective antibodies were generated against unique antigenic peptide sequences form JmJ3C protein, this peptide sequence was not found in any other protein in the gene bank. The Jmj3C antibodies were affinity purified over immobilized antigen based chromatography, and the purified immunoglobulins are stabilized in antibody stabilization buffer. FabGennix Int. Inc., will also provide limited quantities of antigenic blocking peptide for Jmj3C. Antibodies to several other targets invlloved in epigenetic research area are available from FabGennix International Inc. For a complete list of antibodies please visit http://www.fabgennix.com. FabGennix Inc. will conjugate antibodies with secondary enzymes (alk-Pase or HRP) or fluorescent probes upon request at a nominal cost. FabGennix Int. Inc., will also provide western blot positive controls for it antibodies in ready-to-use buffer. Limited quantities of antigenic blocking peptide is available (Please inquire before placing orders).
For research use only, not for diagnostic or therapeutic use.
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