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Anti-Estrogen Receptor α (C-terminus) Antibody

     
  • 1 - Anti-Estrogen Receptor α (C-terminus) Antibody AN1787
    Western blot image of human MCF-7 cells treated with pervanadate (1 mM) for 30 min. (lanes 1-6). Some lanes of the blot were then treated with alkaline phosphatase (lanes 2, 4, & 6). The blot was probed with mouse monoclonal anti-ERα (Tyr-537) phospho-specific (lanes 1 & 2), rabbit polyclonal anti-ERα (C-terminus) (lanes 3 & 4), and rabbit polyclonal anti-ERα (Tyr-537) phospho-specific (lanes 5 & 6).
  • 2 - Anti-Estrogen Receptor α (C-terminus) Antibody AN1787
    Immunocytochemical labeling of Estrogen Receptor α in paraformaldehyde fixed and NP-40 permeabilized MDA-MB-231 cells. The cells were labeled with rabbit polyclonal anti-Estrogen Receptor α (AN1787). The antibody was detected using goat anti-rabbit DyLight® 594.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, ICC, IP
Primary Accession P03372
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 66216 Da
Additional Information
Gene ID 2099
Other Names ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER
Target/Specificity Estrogen receptor α (ERα) is a member of the steroid receptor superfamily and its structure includes an N-terminal ligand-independent transactivation domain (AF-1), a highly conserved DNA binding domain, and a C-terminal ligand-dependent transactivation domain (AF-2). AF-1 and AF-2 activate transcription independently and synergistically, and act in a promoter- and cell-specific manner. Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity. Ser-104, Ser-106, Ser-118, and Ser-167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. In addition to these sites, phosphorylation of Tyr-537 has been implicated in maximal hormone binding, dimerization, and transcriptional activity. Tyr-537, located in the AF-2 domain, is phosphorylated by c-Src leading to nuclear export of ERα and degradation. Thus, a variety of phosphorylation events control ERα activity.
Dilution WB~~1:1000
ICC~~N/A
IP~~N/A
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-Estrogen Receptor α (C-terminus) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Estrogen receptor α (ERα) is a member of the steroid receptor superfamily and its structure includes an N-terminal ligand-independent transactivation domain (AF-1), a highly conserved DNA binding domain, and a C-terminal ligand-dependent transactivation domain (AF-2). AF-1 and AF-2 activate transcription independently and synergistically, and act in a promoter- and cell-specific manner. Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity. Ser-104, Ser-106, Ser-118, and Ser-167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. In addition to these sites, phosphorylation of Tyr-537 has been implicated in maximal hormone binding, dimerization, and transcriptional activity. Tyr-537, located in the AF-2 domain, is phosphorylated by c-Src leading to nuclear export of ERα and degradation. Thus, a variety of phosphorylation events control ERα activity.

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