Render Target: SSR
Render Timestamp: 2025-01-24T19:57:29.611Z
Commit: 8d9f38232df81570bbc23eaa560b31cb39dd8776
XML generation date: 2024-09-20 06:15:48.754
Product last modified at: 2025-01-01T09:05:44.180Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Estrogen Receptor α (62A3) Mouse mAb #2512

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Inquiry Info. # 2512

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 66
    Source/Isotype Mouse IgG2a
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Estrogen Receptor α (62A3) Mouse mAb detects endogenous levels of estrogen receptor α. It does not cross-react with estrogen receptor beta or other family members.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser118 of human ER alpha.

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