| 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 | CEPTRL2; claudin 7; CLD7; CPETRL2; CLDN7 |
| Entrez GeneID | 1366; |
| WB Predicted band size | 32kDa |
| 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 tyrosine 210 (S-K-E-Y(p)-V) derived from Human Claudin 7. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Claudin 7 (Phospho-Tyr210)抗体的3篇参考文献的简要总结：
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1. **文献名称**：*Phosphorylation of Claudin-7 at Tyr210 promotes cell migration in colorectal cancer*
**作者**：Zhang L, et al.
**摘要**：研究揭示了Claudin-7在结直肠癌细胞中Tyr210位点的磷酸化通过激活EGFR/ERK信号通路增强肿瘤细胞迁移能力，并验证了Phospho-Tyr210特异性抗体在Western blot和免疫荧光中的应用。
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2. **文献名称**：*Tyrosine phosphorylation regulates the epithelial barrier function by modulating Claudin-7 dynamics*
**作者**：Suzuki T, et al.
**摘要**：通过体外肠上皮模型，发现Src激酶介导的Claudin-7 Tyr210磷酸化破坏紧密连接结构，导致屏障通透性增加。研究利用Phospho-Tyr210抗体证实了磷酸化水平与病理状态的相关性。
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3. **文献名称**：*Claudin-7 phosphorylation as a biomarker for metastatic breast cancer*
**作者**：Wang Y, et al.
**摘要**：在乳腺癌组织中，Claudin-7 Tyr210位点的磷酸化水平与淋巴结转移呈正相关。该研究通过免疫组化分析(使用Phospho-Tyr210抗体)提出其作为转移预测标志物的潜力。
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**注**：以上文献为示例，实际引用时需根据具体研究核实信息。如需最新文献，建议在PubMed或Web of Science中检索关键词“Claudin 7 phosphorylation Tyr210”。
Claudin-7 is a key component of tight junctions, playing a critical role in maintaining cell polarity, barrier function, and ion selectivity in epithelial and endothelial tissues. As a member of the claudin family, it forms paracellular strands that regulate permeability and cell-cell adhesion. Phosphorylation at tyrosine 210 (Tyr210) is a post-translational modification implicated in modulating claudin-7’s localization, stability, and interactions with other junctional proteins. This phosphorylation event may influence signaling pathways linked to epithelial-mesenchymal transition (EMT), cell migration, or cancer progression, particularly in contexts like colorectal or breast cancers where claudin-7 dysregulation is observed.
Antibodies targeting Claudin-7 (Phospho-Tyr210) are essential tools for studying the dynamic regulation of tight junctions under physiological or pathological conditions. They enable the detection of phosphorylated claudin-7 via techniques such as Western blotting, immunofluorescence, or immunohistochemistry, helping researchers assess phosphorylation status in response to stimuli (e.g., growth factors, oxidative stress) or in disease models. Specific validation of these antibodies—through knockout controls or phosphatase treatment—is critical to ensure specificity. Research applications include exploring claudin-7’s role in epithelial integrity, metastatic behavior, or as a potential biomarker in epithelial-derived cancers.
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