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Technical Data Sheet

EP5431

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Estrogen Receptor α (C-terminus)
Rabbit Polyclonal
Price
Size
Species Reactivity
MW

$245
100 μl
Hu, Rt, Ms
68 kDa

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Enlarge

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).

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Enlarge

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 (EP5431). The antibody was detected using goat anti-rabbit DyLight® 594.

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Application
Dilution


ELISA
1:1000


ICC
1:100


IP
1:50


WB
1:500



End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.
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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.


Background References
Castoria, G. et al. (2012) Oncogene. 31:4868.
Anbalagan M, Rowan BG (2015) Mol Cell Endocrin. 418(3):264.
Immunogen
ERα (C-terminus) synthetic peptide (coupled to carrier protein) corresponds to amino acids in the C-terminus of human ERα. This sequence is well conserved in rat and mouse ERα, but is not found in ERβ.
Buffer and Storage
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Specificity
The antibody was affinity purified using ERα (C-terminus) peptide (without carrier). This antibody detects several forms of ERα ranging from 66 to 35 kDa* on SDS-PAGE immunoblots of MCF-7 cells treated with pervanadate, and MDA-MB-231 cells.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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