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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Estrogen receptor alpha (ESR1) is a ligand-activated nuclear hormone receptor that regulates gene transcription in response to estrogen signaling and plays a central role in the growth and differentiation of hormone-responsive tissues. ESR1 activity is tightly controlled by post-translational modifications, including phosphorylation at multiple regulatory residues that influence receptor stability, localization, and transcriptional output. Among these, serine 118 (S118) is one of the most well-characterized phosphorylation sites and is strongly associated with transcriptional activation of the receptor.
Phospho-ER alpha (pS118) antibody, also referred to as ESR1 pS118 antibody and phosphorylated Estrogen receptor alpha antibody in the literature, recognizes ESR1 specifically when phosphorylated at serine 118. This modification can be induced by estrogen binding as well as by growth factor signaling pathways such as MAPK, linking extracellular cues to nuclear transcriptional responses. Phosphorylation at S118 enhances ESR1 transcriptional activity and promotes expression of estrogen-responsive genes, making it a key marker of receptor activation in both normal physiology and disease.
This Phospho-ER alpha (pS118) Antibody / Hormone-Induced Activation Marker Antibody (clone EIG-5) is uniquely positioned for studies of signaling dynamics and hormone responsiveness. In cellular systems, S118 phosphorylation is rapidly increased following treatment with beta-estradiol or growth factors such as EGF, reflecting convergence of endocrine and mitogenic signaling pathways. This inducible phosphorylation event provides a valuable readout for pathway activation and receptor engagement, particularly in breast cancer models where ESR1 signaling drives tumor growth and therapeutic response.
In tissue-based analyses, phosphorylated ESR1 is typically detected as nuclear staining in epithelial and tumor cells, consistent with its role as a transcription factor. Variation in phospho-ER alpha levels can reflect differences in hormonal status, growth factor signaling, and treatment response, providing insight into tumor biology and pathway activation states. In western blot analysis, phospho-ER alpha is detected at an apparent molecular weight consistent with total ESR1, with increased signal observed under conditions that promote receptor activation.
Clone EIG-5 is a recombinant rabbit monoclonal antibody designed to detect ESR1 phosphorylated at serine 118 with specificity for the modified form of the protein. A phospho-ER alpha antibody is suitable for detecting activation-dependent changes in ESR1 signaling in studies of hormone receptor biology, breast cancer research, and signal transduction.
For comprehensive detection of Estrogen receptor alpha across hormone signaling and breast cancer studies, see our Estrogen Receptor alpha antibody (clone ESR1/3557).
Optimal dilution of the Phospho-ER alpha (pS118) Antibody / Hormone-Induced Activation Marker Antibody should be determined by the researcher.
A synthetic peptide specific to human ER alpha / ESR1 (surrounding pS118) was used as the immunogen for the Phospho-ER alpha (pS118) Antibody.
Store the Phospho-ER alpha (pS118) Antibody at -20oC.
Phospho ER alpha S118 antibody, ESR1 pS118 antibody, Phosphorylated Estrogen receptor alpha antibody, ER alpha phospho S118 antibody, ESR1 activation marker antibody
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