The Phospho-Estrogen Receptor α Antibody Sampler Kit provides an economical means to evaluate the activation status of ERα, including phosphorylation of Ser104/106, Ser167, and Ser118. The monoclonal control ERα antibody is also included to detect total Estrogen Receptor α levels. The kit contains enough primary antibody to perform four Western blot experiments.
Phospho-Estrogen Receptor α (Ser167) (D1A3) Rabbit mAb detects endogeneous levels of ERα protein only when phosphorylated at Ser167, and also cross reacts with a nonspecific band around 77 kDa. Phospho-Estrogen Receptor α (Ser104/106) Antibody detects endogenous levels of Ser104/106 phosphorylated ERα. Phospho-Estrogen Receptor α (Ser118) (16J4) Mouse mAb will detect endogenous levels of Ser118 phosphorylated ERα. Estrogen Receptor α (D8H8) Rabbit mAb detects endogenous levels of ERα. Each antibody in the kit does not cross-react with phosphorylated or nonphosphorylated ER isoforms β or other related family members.
Activation state monoclonal antibodies are produced by immunizing animals with synthetic phosphopeptides or non-phosphopeptide corresponding to residues surrounding Ser167, Ser118, and the carboxy terminus of human estrogen receptor α protein. Activation state polyclonal antibody is produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Ser104/106 of human ERα. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
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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