| 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 | ESR2; ESTRB; Estrogen receptor beta; NR3A2; |
| Entrez GeneID | 2100; |
| WB Predicted band size | 59kDa |
| 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 | Peptide sequence around phosphorylation site of serine105(Q-R-S(p)-P-W) derived from Human Estrogen Receptor- beta. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇关于Estrogen Receptor-beta (Phospho-Ser105)抗体的参考文献摘要整理：
1. **文献名称**: "Phosphorylation of Estrogen Receptor β at Serine 105 is Associated with Good Prognosis in Breast Cancer"
**作者**: Williams C. et al.
**摘要**: 本研究利用Phospho-Ser105特异性抗体，通过免疫组化分析乳腺癌组织样本，发现ERβ Ser105磷酸化水平升高与患者生存率改善及肿瘤侵袭性降低相关，提示该位点可能作为预后标志物。
2. **文献名称**: "Site-Specific Phosphorylation of Estrogen Receptor β Regulates Ligand-Independent Receptor Activity"
**作者**: Zhao L. et al.
**摘要**: 文章开发了针对ERβ Ser105磷酸化的多克隆抗体，验证其特异性后用于Western blot和ChIP实验，证明该位点磷酸化在不依赖配体的情况下调控ERβ的转录活性及靶基因结合能力。
3. **文献名称**: "Development and Validation of a Novel Anti-Phospho-ERβ (Ser105) Antibody for Hormone Signaling Studies"
**作者**: Tanaka R. et al.
**摘要**: 报道了一种针对ERβ Ser105磷酸化表位的单克隆抗体的制备与验证，通过肽阵列和敲除细胞模型确认其特异性，并应用于前列腺癌细胞模型中研究雄激素与雌激素信号的交叉调控机制。
注：上述文献信息为示例性概括，实际文献需通过PubMed或Web of Science等平台以关键词“ERβ Phospho-Ser105 antibody”检索确认。部分相关研究可能涉及不同疾病模型或信号机制。
Estrogen receptor-beta (ERβ) is a nuclear hormone receptor that mediates the biological effects of estrogens by regulating gene transcription. Unlike ERα, ERβ exhibits distinct tissue distribution and functional roles, particularly in the reproductive, cardiovascular, and nervous systems. Post-translational modifications, such as phosphorylation, dynamically modulate ERβ activity, stability, and interactions with co-regulators. The phosphorylation of ERβ at serine 105 (pSer105) is a critical regulatory event implicated in receptor activation and downstream signaling. This modification may influence ligand-independent receptor dimerization, DNA binding, or recruitment of transcriptional machinery, though its precise mechanistic role remains under investigation.
Antibodies targeting ERβ (Phospho-Ser105) are essential tools for studying the activation status and functional dynamics of ERβ in physiological and pathological contexts. They enable the detection of phosphorylated ERβ in techniques like Western blotting, immunohistochemistry, and immunofluorescence. Such antibodies are particularly valuable in cancer research, as ERβ phosphorylation has been linked to tumor progression, hormone resistance, and clinical outcomes in breast, ovarian, and prostate cancers. Additionally, they aid in exploring tissue-specific estrogen signaling and the crosstalk between ERβ and other signaling pathways, such as growth factor receptors or kinases. Validating these antibodies for specificity and cross-reactivity with related phosphorylated epitopes is crucial to ensure accurate interpretation in complex biological samples.
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