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MABN685

Sigma-Aldrich

Anti-KDM4A Antibody, clone5H1

ascites fluid, clone 5H1, from mouse

Synonyme(s) :

Lysine-specific demethylase 4A, JmjC domain-containing histone demethylation protein 3A, Jumonji domain-containing protein 2A, KDM4A

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

5H1, monoclonal

Espèces réactives

human

Technique(s)

immunofluorescence: suitable
immunohistochemistry: suitable
western blot: suitable

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... KDM4A(9682)

Description générale

Lysine methylation of histones is associated with both transcriptionally active chromatin and with silent chromatin, depending on what residue is modified. Histone methyltransferases and demethylases ensure that histone methylations are dynamic and can vary depending on cell cycle or developmental stage. KDM4A demethylates H3K36me3, a modification enriched in the 3′ end of active genes. KDM4A is also known as Lysine-specific demethylase 4A or JmjC domain-containing histone demethylation protein 3A, or Jumonji domain-containing protein 2A, and is encoded by the human gene named KDM4A/JHDM3A/JMJD2/JMJD2A/KIAA0677. KDM4A is the histone demethylase that specifically demethylates ′Lys-9′ and ′Lys-36′ residues of histone H3, thereby playing a central role in histone gene repression, and KDM4A functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated forms. KDM4A does not demethylate histone H3 ′Lys-4′, H3 ′Lys-27′ nor H4 ′Lys-20′, but KDM4A does demethylate trimethylated H3 ′Lys-9′ and H3 ′Lys-36′ residues, while it has no activity on mono- and dimethylated residues. KDM4A also plays a critical role in muscle differentiation as demethylation of various targets allows influences the expression of the Myog gene family critical in muscle cell development. KDMA4A also interacts with histone deacetylases HDAC1, HDAC2, and HCAC3. It is localized in the nucleus and widely expressed. KDM4A’s own levels are mediated via ubiquitination and proteasome degradation. EMD-Millipore’s Anti-KDM4A mouse monoclonal antibody has been tested in western blot on HEK293 and KDM4A transfected HEK293 cell lysates and in paraffin embedded immunohistochemistry on human colon and larynx cancer tissues and in fluorescent immunocytochemistry on NTERA-2 cells in culture.

Immunogène

Purified recombinant fragment of human KDM4A expressed in E. Coli.

Application

Anti-KDM4A Antibody, clone5H1 is a highly specific mouse monoclonal antibody, that targets Jumonji domain-containing protein (JMJD) & has been tested in western blotting, IHC & Immunofluorescence.
Immunohistochemistry Analysis: A 1:200-1,000 dilution from a representative lot detected KDM4A in human colon cancer and larynx cancer tissues.

Immunofluorescence Analysis: A 1:200-1,000 dilution from a representative lot detected KDM4A in NTERA-2 cells.

Optimal working dilutions must be determined by end user.

Qualité

Evaluated by Western Blotting in HEK293 and KDM4A-hIgGFc transfected HEK293 cell lysates.

Western Blotting Analysis: A 1:500-2,000 dilution of this antibody detected KDM4A-hIgGFc transfected HEK293 cell lysates.

Description de la cible

~72 kDa observed

Remarque sur l'analyse

Control
HEK293 and KDM4A-hIgGFc transfected HEK293 cell lysates

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Jialiang Shao et al.
The EMBO journal, 40(20), e107480-e107480 (2021-07-17)
The mTORC1 pathway plays key roles in regulating various biological processes, including sensing amino acid deprivation and driving expression of ribosomal protein (RP)-coding genes. In this study, we observed that depletion of glutamate dehydrogenase 1 (GDH1), an enzyme that converts

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