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Key Documents

SRP0319

Sigma-Aldrich

JMJD2A active human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Sinónimos:

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.

NM_014663

UniProt accession no.

O75164

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.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

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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Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.
Huang Y
Science, 312, 5774-5774 (2006)
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
Ng SS
Nature, 448, 87-91 (2007)
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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