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Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 0.5 to 1.0 µg/ml antibody dilution for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
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Application References:
1. Wang Y, et al. 2010. J. Biol Chem. 21:15668. PubMed
Hela (1) and HepG2 (2) cell nuclear extract were resolved by electrophoresis, transferred to nitrocellulose, and probed with purified anti-RORa antibody. Proteins were visualized using donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Retinoid related orphan receptor alpha (ROR alpha) is a NR1 Thyroid Hormone Like Receptor. Three different subtypes ROR alpha, beta, and gamma have been discovered. ROR alpha plays a key role in the development of the cerebellum. Deletion of ROR alpha in mice causes severe impairment in the differentiation of cerebellar Purkinje neurons and results in the "staggerer" phenotype. ROR alpha has been suggested in the regulation of a number of other physiological processes, including bone formation. Recently, ROR alpha was reported to regulate lymphocyte development and mediate Th17 differentiation synergistically with ROR gamma.
Other Names:
Retinoid related orphan receptor alpha
Structure:
RORs contains four major functional domains: an amino-terminal domain, DNA-binding domain(DBD), a hinge domain and a ligand-binding domina (LBD).
Distribution:
nuclear, Th17 cells
Function:
It can bind as a monomer or as a homodimer to hormone response elements upstream of several genes to enhance the expression of those genes.
Ligand Receptor:
Possible ligands include cholesterol, cholesterol sulfate or other (sulfated) lipid metabolites.
Interaction:
It has been shown that RORa can recruit b-catenin and p300 as co-activators to some promoters.
Antigen References:
1. Dzhagalov I, et al. 2004. 173:2952 2. Yang XO, et al. 2008. Immunity 28:29.
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Purified Anti-RORα
Hela (1) and HepG2 (2) cell nuclear extract were resolved by electrophoresis, transferred to nitrocellulose, and probed with purified anti-RORa antibody. Proteins were visualized using donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.