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SRP0123

Sigma-Aldrich

JMJD2C Active human

recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)

Synonyme(s) :

GASC1, Gene amplified in squamous cell carcinoma 1 protein, JHDM3C, KIAA0780, Lysine-specific demethylase 4C (KDM4C)

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About This Item

Code UNSPSC :
12352200

Source biologique

human

Produit recombinant

expressed in baculovirus infected insect cells

Pureté

≥80% (SDS-PAGE)

Forme

aqueous solution

Poids mol.

69 kDa

Conditionnement

pkg of 100 μg

Concentration

>0.02 mg/mL

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... KDM4C(23081)

Description générale

JMJD2C (Jumonji domain containing), also known as KDM4C (lysine demethylase 4C), is an H3K9me3 demethylase belonging to the conserved family of H3K9me3 erasers, KDM4 demethylases. KDM4 family was first identified in 2006, and is composed of six members namely KDM4A, -B, -C, -D, -E, and -F. This protein predominantly resides at H3K4me3-containing promoter region. JMJD2C protein has multiple reader domains, including a hybrid tandem tudor domain (TTD) and two PHDs (plant homeodomain) of unknown function.
Human JMJD2C, GenBank Accession No. BC143571) (amino-acids 2-372) with N-terminal ST tag, MW = 69kDa, expressed in a Baculovirus infected Sf9 cell expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Actions biochimiques/physiologiques

JMJD2C (Jumonji domain containing), also known as KDM4C (lysine demethylase 4C), is a type of KDM4 demethylases that are responsible for the demethylation of H3K9me2/3, H3K36me3/2, and H1.4K26me3/2. This is accomplished through a hydroxylation reaction requiring the cofactors Fe(II) and 2-oxoglutarate (2-OG). These proteins show heightened expression and activity in multiple types of cancers, and hence, are also classified as oncogenes. KDMA4 family members are capable of coregulating hormone receptors, and hence, are implicated in the progression of hormone dependent cancers, such as breast and prostate cancer. JMJD2C is essential for regulating the expression of growth promoting proteins and the survival factor FRA1 (Fos-related antigen 1) and cyclin D1, and BCL2 (B-cell lymphoma) respectively. The expression of JMJD2C is increased in colon cancer cell, where it interacts with the oncogenic protein β-catenin, the up-regulation of which is essential for the pathogenesis of colon cancer.

Définition de l'unité

One unit is defined as the amount of enzyme required to demethylate 1 pmol of substrate/min at 37°C.

Forme physique

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 20% glycerol and 3 mM DTT.

Notes préparatoires

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Lindsey R Pack et al.
The Journal of biological chemistry, 291(12), 6060-6070 (2016-01-10)
Histone H3 lysine 4 trimethylation (H3K4me3) and histone H3 lysine 9 trimethylation (H3K9me3) are epigenetic marks with opposing roles in transcription regulation. Whereas colocalization of these modifications is generally excluded in the genome, how this preclusion is established remains poorly
Ulrike Leurs et al.
ACS chemical biology, 9(9), 2131-2138 (2014-07-12)
Inhibition of histone demethylases has within recent years advanced into a new strategy for treating cancer and other diseases. Targeting specific histone demethylases can be challenging, as the active sites of KDM1A-B and KDM4A-D histone demethylases are highly conserved. Most
Pro-growth role of the JMJD2C histone demethylase in HCT-116 colon cancer cells and identification of curcuminoids as JMJD2 inhibitors.
Kim TD et al
American Journal of Translational Research, 6(3), 236-247 (2014)

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