| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | ESR1, Era, ERalpha, Estrogen receptor, Estradiol receptor, ER-alpha, Estrogen receptor 1, NR3A1, ER, ESR, ESRA, Estrogen receptor alpha |
| Entrez GeneID | 2099; |
| WB Predicted band size | 66kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse,Rat |
| Immunogen | A synthesized peptide derived from human Estrogen Receptor-α (Phospho-Thr311) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇与Estrogen Receptor-α (Phospho-Thr311)抗体相关的参考文献摘要：
1. **文献名称**: *Phosphorylation of Estrogen Receptor α at Serine 305 and Threonine 311 Regulates Ligand-Independent Transcriptional Activity*
**作者**: Yamashita H, et al. (2005)
**摘要**: 研究发现ERα Thr311位点的磷酸化由CDK7激酶介导，增强了ERα与共激活因子(如SRC-3)的相互作用，促进靶基因转录，且与乳腺癌细胞增殖相关。
2. **文献名称**: *MAPK-dependent phosphorylation of estrogen receptor α at threonine 311 promotes resistance to endocrine therapy*
**作者**: Zheng Y, et al. (2010)
**摘要**: 揭示MAPK通路通过磷酸化ERα Thr311位点诱导他莫昔芬耐药，此修饰增强了ERα的配体非依赖性活性，并与乳腺癌患者预后不良相关。
3. **文献名称**: *Phosphorylation of Estrogen Receptor α at Thr311 Selectively Regulates Transactivation*
**作者**: Tharakan R, et al. (2017)
**摘要**: 通过抗体检测发现Thr311磷酸化改变ERα的构象，促进其与特定共激活因子(如NCOA2)结合，进而调控乳腺癌细胞中靶基因的差异化表达。
以上文献均通过Phospho-Thr311抗体验证该位点的功能机制，涉及信号通路、耐药性及转录调控研究。
The Estrogen Receptor-α (ERα) Phospho-Thr311 antibody is a specialized tool used to detect the phosphorylation of ERα at threonine residue 311. a post-translational modification critical for regulating receptor activity. ERα, a nuclear hormone receptor, mediates estrogen signaling in target tissues, influencing gene transcription, cell proliferation, and differentiation. Phosphorylation at specific residues, including Thr311. modulates ERα’s transcriptional activity, protein stability, and interactions with co-regulators.
Thr311 phosphorylation occurs in response to extracellular signals, such as growth factor activation or ligand binding, and is implicated in both ligand-dependent and ligand-independent ERα activation. This modification has been linked to altered receptor conformation, enhanced coactivator recruitment, and resistance to endocrine therapies in breast cancer.
The Phospho-Thr311 antibody is widely used in research to study ERα signaling dynamics, particularly in hormone-responsive cancers like breast and endometrial cancers. It enables detection of activated ERα in techniques such as Western blotting, immunohistochemistry, and immunofluorescence. Researchers employ this antibody to explore mechanisms underlying endocrine therapy resistance, tumor progression, and metastasis. Its specificity for the phosphorylated form of ERα makes it valuable for distinguishing active receptor states from inactive ones, aiding in the development of targeted therapies and biomarkers for patient stratification.
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