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Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
MOLT-4 nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-RARα antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
RARα (retinoic acid receptor alpha) is a 51 kD member of the nuclear hormone receptor family, NR1 subfamily. This nuclear protein contains modulating, DNA-binding, and steroid binding domains, and has been reported to have multiple isoforms. RARα is a nuclear receptor for retinoic acid that controls cell function by regulating gene expression and inducing profound effects on vertebrate development, acting as a morphogen and powerful teratogen. RARα is increased by protein kinase C stimulation, and estrogen; decreased at G0/G1 to S phase of cell cycle and in lymphocytes by cellular activation. RARα can be modified by phosphorylation and has been shown to interact with NCOA3 and NCOA6 co-activators leading to strong increases in the transcription of target genes. The Poly6168 antibody recognizes the N-terminal region of human RARα and has been shown to be useful for Western blotting.
Nuclear receptor for retinoic acid, controls cell function by regulating gene expression. Induces profound effects on vertebrate development; morphogen and powerful teratogen
Regulation:
Increased by protein kinase C stimulation, estrogen; decreased at G0/G1 to S phase of cell cycle and in lymphocytes by cellular activation
Modification:
Phosphorylation
Interaction:
NCOA3 and NCOA6 co-activators, leads to strong increase in transcription of target genes
Antigen References:
1. Giguere V, et al. 1987. Nature 330:624. 2. Petkovich M, et al. 1987. Nature 330:444.
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Purified anti-RARα
MOLT-4 nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-RARα antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
