JARID1A Antibody [E24E4] | Primary Antibodies

Application: Reactivity: Mouse, Human

Lane 1: HeLa, Lane 2: HeLa (KO KDM5A), Lane 3: 3T3, Lane 4: HEK293

Usage Information

Dilution
WB1:5000 IP1:100 IF1:2000 FCM1:1500

Application
WB, IP, IF, FCM

Reactivity
Mouse, Human

Source
Rabbit Monoclonal Antibody

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

Predicted MW Observed MW
161 kDa, 22-46 kDa 162-240 kDa, 43 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Mouse testis; HEK-293 cells; NIH/3T3 cells; HeLa cells; LLC cells; HAP1 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
JARID1A Antibody [E24E4] detects endogenous levels of total JARID1A protein.

Clone
E24E4

Synonym(s)
JARID1A; RBBP2; RBP2; KDM5A; Lysine-specific demethylase 5A; Histone demethylase JARID1A; Jumonji/ARID domain-containing protein 1A; Retinoblastoma-binding protein 2; [histone H3]-trimethyl-L-lysine(4) demethylase 5A; RBBP-2

Background
JARID1A (also known as KDM5A or RBP2), a JmjC domain-containing histone H3K4 demethylase, plays a pivotal role in epigenetic regulation by removing di- and tri-methyl marks from H3K4 to repress transcription at active promoters, featuring a multi-domain architecture including an N-terminal JmjN domain for catalytic coordination with the core JmjC domain requiring Fe(II) and α-ketoglutarate, an intervening ARID domain that binds GC-rich DNA motifs like CCGCCC via its L1 loop to target nucleosomes, PHD1-3 fingers where PHD1 recognizes unmodified H3K4 to stabilize repression in a feed-forward loop, a C5HC2 zinc finger enhancing demethylase activity, and plant homeodomain fingers facilitating histone tail interactions. JARID1A interacts with RB to enforce E2F repression during G1/S transition, joins NuRD and SIN3B complexes to coordinate deacetylation and remodeling via CHD4 for cell cycle gene control, accumulates at γ-H2AX foci post-DNA damage to reduce H3K4me3 without impairing double-strand break repair, and modulates circadian rhythm by enhancing CLOCK-BMAL1 cyclic transcription independently of demethylation, while in hematopoiesis it binds GATA1 via PHD2 to drive erythroid differentiation and proliferation, with NUP98-JARID1A fusions driving myeloid leukemia through aberrant H3K4 demethylation and pathway activation. Its overexpression promotes cancer progression by sustaining PI3K/Akt signaling via PTEN suppression, advancing the G1/S phase through Cyclin D1 upregulation and repressing let-7e miRNA, and inducing drug-tolerant states via HDAC interplay.

Background

JARID1A (also known as KDM5A or RBP2), a JmjC domain-containing histone H3K4 demethylase, plays a pivotal role in epigenetic regulation by removing di- and tri-methyl marks from H3K4 to repress transcription at active promoters, featuring a multi-domain architecture including an N-terminal JmjN domain for catalytic coordination with the core JmjC domain requiring Fe(II) and α-ketoglutarate, an intervening ARID domain that binds GC-rich DNA motifs like CCGCCC via its L1 loop to target nucleosomes, PHD1-3 fingers where PHD1 recognizes unmodified H3K4 to stabilize repression in a feed-forward loop, a C5HC2 zinc finger enhancing demethylase activity, and plant homeodomain fingers facilitating histone tail interactions. JARID1A interacts with RB to enforce E2F repression during G1/S transition, joins NuRD and SIN3B complexes to coordinate deacetylation and remodeling via CHD4 for cell cycle gene control, accumulates at γ-H2AX foci post-DNA damage to reduce H3K4me3 without impairing double-strand break repair, and modulates circadian rhythm by enhancing CLOCK-BMAL1 cyclic transcription independently of demethylation, while in hematopoiesis it binds GATA1 via PHD2 to drive erythroid differentiation and proliferation, with NUP98-JARID1A fusions driving myeloid leukemia through aberrant H3K4 demethylation and pathway activation. Its overexpression promotes cancer progression by sustaining PI3K/Akt signaling via PTEN suppression, advancing the G1/S phase through Cyclin D1 upregulation and repressing let-7e miRNA, and inducing drug-tolerant states via HDAC interplay.

References
https://pubmed.ncbi.nlm.nih.gov/26645689/ https://pubmed.ncbi.nlm.nih.gov/37838974/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%