Datasheet

Biological Description

Specificity	JMJD2A Antibody [B12L5] detects endogenous levels of total JMJD2A protein.
Background	JMJD2A, a member of the Jumonji C (JmjC) domain-containing histone demethylase family, is a pivotal epigenetic regulator that modulates gene expression through chromatin remodeling. JMJD2A contains several conserved domains, including two leukemia-associated protein/plant homeodomain (LAP/PHD) zinc fingers, one JmjN domain, a JmjC catalytic domain, and two Tudor domains; the Tudor domains specifically recognize methylated histones such as H3K4, H3K9, and H4K20, facilitating chromatin targeting. The JmjC domain mediates demethylase activity via an iron- and α-ketoglutarate-dependent oxidative mechanism that removes tri- and dimethyl groups from lysine residues on histone H3, predominantly targeting H3K9 and H3K36. The catalytic core structure shows a highly specific substrate recognition involving the main chain interactions and a proline-induced bent conformation of the histone peptide for optimal fit into the active pocket, dictating enzymatic specificity. JMJD2A plays dual roles in transcriptional activation and repression by interacting with retinoblastoma protein (pRb) and histone deacetylases (HDACs), thereby modulating E2F-regulated promoters and influencing cell proliferation and oncogenesis. Overexpression and dysregulation of JMJD2A are linked to multiple cancers.

Specificity

JMJD2A Antibody [B12L5] detects endogenous levels of total JMJD2A protein.

Background

JMJD2A, a member of the Jumonji C (JmjC) domain-containing histone demethylase family, is a pivotal epigenetic regulator that modulates gene expression through chromatin remodeling. JMJD2A contains several conserved domains, including two leukemia-associated protein/plant homeodomain (LAP/PHD) zinc fingers, one JmjN domain, a JmjC catalytic domain, and two Tudor domains; the Tudor domains specifically recognize methylated histones such as H3K4, H3K9, and H4K20, facilitating chromatin targeting. The JmjC domain mediates demethylase activity via an iron- and α-ketoglutarate-dependent oxidative mechanism that removes tri- and dimethyl groups from lysine residues on histone H3, predominantly targeting H3K9 and H3K36. The catalytic core structure shows a highly specific substrate recognition involving the main chain interactions and a proline-induced bent conformation of the histone peptide for optimal fit into the active pocket, dictating enzymatic specificity. JMJD2A plays dual roles in transcriptional activation and repression by interacting with retinoblastoma protein (pRb) and histone deacetylases (HDACs), thereby modulating E2F-regulated promoters and influencing cell proliferation and oncogenesis. Overexpression and dysregulation of JMJD2A are linked to multiple cancers.

Usage Information

Application

WB, IP, IHC, IF

Dilution

WB	IP	IHC	IF
1:1000	1:100	1:100	1:200

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

150 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/15927959/
https://pubmed.ncbi.nlm.nih.gov/17567753/

JMJD2A Antibody [B12L5]

Biological Description

Usage Information

References

Application Data