Synthetic phosphopeptide derived from human ERalpha around the phosphorylation site of Serine 118.
Conjugation:
Unconjugated
Alternative Names:
Estrogen receptor, ER-alpha, ER, ESR1, ESR, NR3A1
Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ERalpha and ERbeta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus , though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ERalpha and ERbeta have been shown to be differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ERalpha and ERbeta may be regulated by distinct mechanisms even though they share many functional characteristics.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC:1:50~1:200
Application Notes:
p-ERalpha (S118) polyclonal antibody detects endogenous levels of ERalpha protein only when phosphorylated at Ser118
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