Phospho-Estrogen Receptor alpha (S118) Recombinant Rabbit mAb IgG

SKU: BA111634-100µl
$279.00Price

Fig1: Western blot analysis of Estrogen Receptor alpha(phospho S118) on MCF-7 cell lysates using anti- phospho-Estrogen Receptor alpha(S118) antibody at 1/1,000 dilution.

Fig2: ICC staining phospho-Estrogen Receptor alpha(S118) in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig3: ICC staining phospho-Estrogen Receptor alpha(S118) in MCF-7 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Bon Opus Cat. #BA111634
Size
  • Host Species; Species Reactivity

    Rabbit; Human
  • Immunogen

    Synthetic phospho-Peptide corresponding to residues surrounding Ser118 of human Estrogen Receptor alpha.
  • Application Summary

    WB, ICC/IF, IHC
  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Estrogen receptor, ER-alpha, Estradiol receptor, Nuclear receptor subfamily 3 group A member 1
  • Background

    Estrogen receptor alpha (ERa, ER, ESR, ESRA, Era, NR3A1, estrogen receptor 1) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding and activation of transcription. Alternative splicing results in several ERa mRNA transcripts, which differ primarily in their 5' untranslated regions. ERa undergoes phosphorylation in response to estradiol binding. Human ERa is predominately phosphorylated on Ser 118 and to a lesser extent on Ser 104 and Ser 106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser 118 and Ser 167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERa. In contrast, activation of protein kinase A increases the phosphorylation of Ser 236, which is located in the DNA-binding domain. Src kinase-dependent Tyr 537 phosphorylation may enhance estrogen binding to ERa. Mutation of Tyr 537 of the human ERa produces receptors having a range of constitutive activity.(ET1610-32)

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