Specificity
Overexpressed in several esophageal squamous cell carcinomas (ESCs).
Tag/Conjugate
Unconjugated
Alternative Names
The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails.
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.
Antigen Description
This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein with one JmjC domain, one JmjN domain, two PHD-type zinc fingers, and two Tudor domains. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form. Chromosomal aberrations and increased transcriptional expression of this gene are associated with esophageal squamous cell carcinoma. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2009]
Function
androgen receptor binding; dioxygenase activity; enzyme binding; histone demethylase activity (H3-K9 specific); histone demethylase activity (H3-K9 specific); zinc ion binding;
Synonyms
KDM4C; lysine (K)-specific demethylase 4C; GASC1; JHDM3C; JMJD2C; TDRD14C; bA146B14.1; lysine-specific demethylase 4C; GASC-1 protein; tudor domain containing 14C; jumonji domain containing 2C; jumonji domain-containing protein 2C; gene amplified in squamous cell carcinoma 1 protein; JmjC domain-containing histone demethylation protein 3C;
Citations
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Zhao, M; Liang, G; et al. Abnormal epigenetic modifications in peripheral blood mononuclear cells from patients with alopecia areata. BRITISH JOURNAL OF DERMATOLOGY 166:266-273(2012).
Leurs, U; Lohse, B; et al. Substrate- and Cofactor-independent Inhibition of Histone Demethylase KDM4C. ACS CHEMICAL BIOLOGY 9:2131-2138(2014).