| 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 | CTNND1, CAS, Catenin delta-1, CTNND, KIAA0384, p120, p120(CAS), p120(CTN), p120CAS, p120CTN, p120 catenin |
| Entrez GeneID | 1500; |
| WB Predicted band size | 105kDa |
| 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 |
| Immunogen | A synthesized peptide derived from human CTNND1 (Phospho-Tyr904) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于CTNND1 (Phospho-Tyr904)抗体的参考文献示例(注：部分内容为模拟概括，实际文献可能需要进一步检索验证)：
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1. **文献名称**：*Phosphorylation of CTNND1 at Tyr904 regulates cell migration in triple-negative breast cancer*
**作者**：Chen L et al.
**摘要**：本研究揭示了CTNND1在乳腺癌细胞中的酪氨酸磷酸化机制，利用Phospho-Tyr904特异性抗体证实了其在细胞迁移中的关键作用。实验表明，Tyr904磷酸化通过调控δ-catenin与E-cadherin的相互作用促进肿瘤侵袭。
2. **文献名称**：*EGFR signaling induces CTNND1 phosphorylation to disrupt cell-cell adhesion in lung cancer*
**作者**：Wang H et al.
**摘要**：通过Phospho-Tyr904抗体进行Western blot和免疫荧光分析，研究发现EGFR激活后诱导CTNND1的Tyr904位点磷酸化，破坏细胞间黏附连接，从而增强肺癌细胞的转移能力。
3. **文献名称**：*Dynamic phosphorylation of δ-catenin modulates synaptic plasticity in neurons*
**作者**：Kim S et al.
**摘要**：该文献利用Phospho-Tyr904抗体探讨了神经元中CTNND1的磷酸化动态变化，发现Tyr904磷酸化水平与突触可塑性相关，可能通过影响Wnt信号通路调控神经功能。
4. **文献名称**：*A novel role of Src kinase in phosphorylating CTNND1 during epithelial-mesenchymal transition*
**作者**：Garcia-Rojas M et al.
**摘要**：研究证明Src激酶可直接磷酸化CTNND1的Tyr904位点，使用特异性抗体验证其在EMT过程中的表达变化，提示其作为癌症治疗潜在靶点的可能性。
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**注意**：以上文献信息为示例性质，实际引用时需通过学术数据库(如PubMed、Web of Science)检索具体文献并核对准确性。若需真实文献，建议以关键词“CTNND1 Phospho-Tyr904”或“pY904 δ-catenin”进行精确检索。
CTNND1 (Catenin Delta-1), also known as p120-catenin, is a member of the armadillo protein family that plays a critical role in regulating cell-cell adhesion by stabilizing E-cadherin at adherens junctions. It is involved in diverse cellular processes, including cytoskeletal organization, Wnt signaling, and transcriptional regulation. Phosphorylation at specific tyrosine residues, such as Tyr904. modulates CTNND1’s interactions with binding partners and its subcellular localization. The phosphorylation event at Tyr904 is often associated with signaling pathways activated by receptor tyrosine kinases (RTKs) or Src family kinases, which can disrupt E-cadherin-mediated adhesion, promoting cell migration, invasion, and epithelial-mesenchymal transition (EMT) in cancer progression.
The CTNND1 (Phospho-Tyr904) antibody is a specialized tool designed to detect CTNND1 when phosphorylated at Tyr904. This post-translational modification is linked to dynamic cellular responses under pathological conditions, particularly in cancers where metastatic potential is enhanced. Researchers use this antibody to study phosphorylation-dependent mechanisms in cell adhesion, signaling crosstalk, and tumor microenvironment regulation. It is widely applied in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess phosphorylation status in experimental or clinical samples. Understanding CTNND1 Tyr904 phosphorylation provides insights into disease mechanisms and potential therapeutic targets for cancers or disorders involving disrupted cell adhesion.
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