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Technical Data Sheet

EM5451

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Estrogen Receptor α (Tyr-537), phospho-specific
Mouse Monoclonal IgG1
Price
Size
Species Reactivity
MW

$295
100 μl
Hu, Rt, Ms, Ck, Fr
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).

Application
Dilution


ELISA
1:2000


WB
1:1000



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
Clone M545 was generated from a phospho-ERα (Tyr-537) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Tyr-537 in human ERα. This sequence is well conserved in rat and mouse ERα, and is also well conserved in ERβ (Tyr-488).
Buffer and Storage
Mouse monoclonal, 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 phospho-ERα (Tyr-537) 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 this reactivity is removed after alkaline phosphatase treatment.

*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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SM2591
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SM2611
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