RARα Antibody [M12K22] | Primary Antibodies

Application: Reactivity: Human, Mouse, Monkey

Lane 1: T47D, Lane 2: MCF7, Lane 3: HepG2

Usage Information

Dilution
WB1:1000 IP1:100 CHIP1:50

Application
WB, IP, ChIP

Reactivity
Human, Mouse, Monkey

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
60 kDa

Datasheet & SDS

Biological Description

Specificity
RARα Antibody [M12K22] detects endogenous levels of total RARα protein.

Clone
M12K22

Synonym(s)
Retinoic acid receptor alpha; RAR-alpha; Nuclear receptor subfamily 1 group B member 1; RARA; NR1B1

Background
RARα (retinoic acid receptor alpha), a founding member of the nuclear receptor superfamily alongside RARβ/γ and RXR isoforms, functions primarily as an RXR heterodimeric transcription factor that senses all-trans retinoic acid (ATRA) to regulate gene expression critical for embryonic patterning, hematopoiesis, and epithelial differentiation. Its modular architecture includes a DNA-binding domain with two zinc fingers for retinoic acid response element (RARE) recognition and a ligand-binding domain that undergoes conformational rearrangement upon ATRA binding to exchange corepressors (NCoR/HDAC) for coactivators (SRC/p300). In the absence of ligand, RARα-RXR silences target genes like HOX clusters and Cdx1 through HDAC-mediated chromatin compaction, whereas ATRA binding induces helix 12 repositioning, CBP recruitment, and H3K14 acetylation to activate transcription while promoting receptor phosphorylation by JNK and proteasomal turnover for signal termination. This dynamic switches integrate with Wnt/β-catenin antagonism, where RARα represses LEF/TCF targets, and TGF-β/Smad pathways via direct heterodimerization, fine-tuning mesenchymal-to-epithelial transitions during development and curtailing aberrant proliferation in keratinocytes. RARα governs granulopoiesis, limb bud outgrowth, and skin barrier formation, positioning it as a key effector for researchers modeling retinoid pharmacodynamics in APL patient-derived xenografts or dissecting squamous differentiation via ChIP-seq in organotypic cultures. The t(15;17) PML-RARα fusion in acute promyelocytic leukemia constitutively recruits corepressors to RAREs, blocking differentiation until supraphysiologic ATRA doses relieve repression, unveiling its therapeutic vulnerability.

Background

RARα (retinoic acid receptor alpha), a founding member of the nuclear receptor superfamily alongside RARβ/γ and RXR isoforms, functions primarily as an RXR heterodimeric transcription factor that senses all-trans retinoic acid (ATRA) to regulate gene expression critical for embryonic patterning, hematopoiesis, and epithelial differentiation. Its modular architecture includes a DNA-binding domain with two zinc fingers for retinoic acid response element (RARE) recognition and a ligand-binding domain that undergoes conformational rearrangement upon ATRA binding to exchange corepressors (NCoR/HDAC) for coactivators (SRC/p300). In the absence of ligand, RARα-RXR silences target genes like HOX clusters and Cdx1 through HDAC-mediated chromatin compaction, whereas ATRA binding induces helix 12 repositioning, CBP recruitment, and H3K14 acetylation to activate transcription while promoting receptor phosphorylation by JNK and proteasomal turnover for signal termination. This dynamic switches integrate with Wnt/β-catenin antagonism, where RARα represses LEF/TCF targets, and TGF-β/Smad pathways via direct heterodimerization, fine-tuning mesenchymal-to-epithelial transitions during development and curtailing aberrant proliferation in keratinocytes. RARα governs granulopoiesis, limb bud outgrowth, and skin barrier formation, positioning it as a key effector for researchers modeling retinoid pharmacodynamics in APL patient-derived xenografts or dissecting squamous differentiation via ChIP-seq in organotypic cultures. The t(15;17) PML-RARα fusion in acute promyelocytic leukemia constitutively recruits corepressors to RAREs, blocking differentiation until supraphysiologic ATRA doses relieve repression, unveiling its therapeutic vulnerability.

References
https://pubmed.ncbi.nlm.nih.gov/9380732/ https://pubmed.ncbi.nlm.nih.gov/21245861/

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%