Estrogen Receptor α Activation Antibody Sampler Kit #49757
Product Information
Kit Usage Information
Protocols
Product Description
The Estrogen Receptor α Activation Antibody Sampler Kit provides an economical means of detecting the activation of estrogen receptor α using phospho-specific and control antibodies. This kit includes enough antibodies to perform two western blot experiments with each primary antibody.
Specificity / Sensitivity
Estrogen Receptor α (D8H8) Rabbit mAb recognizes endogenous levels of total ERα protein. Phospho-Estrogen Receptor α (Ser118) (16J4) Mouse mAb detects endogenous levels of ERα protein only when phosphorylated at Ser118. It does not cross-react with phosphorylated estrogen receptor β. Phospho-Estrogen Receptor α (Ser167) (D5W3Z) Rabbit mAb recognizes endogenous levels of ERα protein only when phosphorylated at Ser167.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues in the carboxy terminus of human ERα protein. Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser118 of human ERα protein. Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser167 of human ERα protein.
Background
Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 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. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).
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- Chen, D. et al. (2000) Mol Cell 6, 127-37.
- Joel, P.B. et al. (1998) Mol Cell Biol 18, 1978-84.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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