SRP0319
JMJD2A active human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Synonym(s):
JHDM3A, KDM4A, lysine (K)-specific demethylase 4A
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
biological source
human
recombinant
expressed in E. coli
assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
42 kDa
packaging
pkg of 100 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
1 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... KDM4A(9682)
General description
Human JMJD2A, also known as JHDM3A and KDM4A (GenBank Accession No. NM_014663), amino-acids 1-350 with N-terminal His-tag, MW=42 kDa, expressed in an E.coli expression system.
JMJD2A (Jumonji domain containing 2A) belongs to the conserved family of Jmjc domain-containing proteins, which in turn are a part of the Jmjc domain histone demethylase superfamily. JMJD2A protein is composed of 1064 amino acids, and contains JmjN and JmjC domains in the catalytic core, a linker region of 350 residues, two plant homeodomains (PHD), and a double Tudor domain. It is one of the six JMJD2 homologs found in humans, ranging from JMJD2A to JMJD2F. It is a trimethyllysine-specific JmjC histone demethylase (HDM).
Biochem/physiol Actions
JMJD2A (Jumonji domain containing 2A) acts as a repressor of transcription, and interacts with histone deacetylase complexes and Rb (retinoblastoma) protein. In histone H3, H3K9me2/3 and H3K36me2/3, this protein is responsible for the demethylation of di- and trimethylated Lys9 and Lys36 residues. It is up-regulated in breast cancer and is responsible for the transcriptional repression of the tumor suppressor ARHI (aplasia Ras homolog member I) which eventually promotes breast cancer proliferation, migration and invasion.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
Ng SS
Nature, 448, 87-91 (2007)
Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.
Huang Y
Science, 312, 5774-5774 (2006)
Dianzheng Zhang et al.
Molecular and cellular biology, 25(15), 6404-6414 (2005-07-19)
Corepressor N-CoR (nuclear receptor corepressor) and the highly related protein SMRT (silencing mediator of retinoid and thyroid hormone receptor) play important roles in different biological processes including proliferation, differentiation, and development. Understanding the biological function of these corepressors requires identification
Jean-François Couture et al.
Nature structural & molecular biology, 14(8), 689-695 (2007-06-26)
JMJD2A is a JmjC histone demethylase (HDM) that catalyzes the demethylation of di- and trimethylated Lys9 and Lys36 in histone H3 (H3K9me2/3 and H3K36me2/3). Here we present the crystal structures of the JMJD2A catalytic domain in complex with H3K9me3, H3K36me2
Steven G Gray et al.
The Journal of biological chemistry, 280(31), 28507-28518 (2005-06-02)
To effectively direct targeted repression, the class I histone deacetylases (HDACs) associate with many important regulatory proteins. In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its
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