Render Target: STATIC
Render Timestamp: 2024-12-26T11:35:13.916Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:55:22.308
Product last modified at: 2024-12-17T18:54:29.198Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-Estrogen Receptor α (Ser167) (D5W3Z) Rabbit mAb (ChIP Formulated) #42101

Filter:
  • ChIP
  • C&R

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • ChIP-Chromatin Immunoprecipitation 
    • C&R-CUT & RUN 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    For optimal ChIP results, use 5 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.

    The CUT&RUN dilution was determined using CUT&RUN Assay Kit #86652.

    Application Dilution
    Chromatin IP 1:100
    CUT&RUN 1:100

    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

    Phospho-Estrogen Receptor α (Ser167) (D5W3Z) Rabbit mAb (ChIP Formulated) recognizes endogenous levels of ERα protein only when phosphorylated at Ser167.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide 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).

    ERα can be phosphorylated at Ser167 by various kinases such as S6K1, RSK, and Aurora A (7-9). Phosphorylation on Ser167 promotes ERα-dependent transcription and cellular proliferation, and is attributed to increased resistance to tamoxifen treatment (6, 9, 10). Various studies have shown that increased Ser167 phosphorylation correlates with poor prognosis in different cancer types (11, 12)
    For Research Use Only. Not For Use In Diagnostic Procedures.
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