| WB | 1/1000 | 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 | Smoothened homolog, SMO, Protein Gx, SMO, SMOH |
| Entrez GeneID | 6608 |
| WB Predicted band size | 86.4kDa |
| 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 |
| Immunogen | This SMO antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 539-567 amino acids from the Central region of human SMO. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇关于SMO抗体的参考文献概括(注：内容基于领域内常见研究方向模拟生成，非真实文献)：
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1. **文献名称**：Development of a High-Affinity Anti-Smoothened Antibody for Hedgehog Pathway Inhibition
**作者**：Chen, X. et al.
**摘要**：研究团队开发了一种新型单克隆SMO抗体，通过噬菌体展示技术筛选获得。该抗体能特异性结合SMO蛋白的细胞外结构域，有效抑制Hedgehog信号通路，在髓母细胞瘤模型中显著降低肿瘤生长速率。
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2. **文献名称**：SMO Expression Profiling in Basal Cell Carcinoma Using Immunohistochemistry
**作者**：Kim, J.H. & Park, S.
**摘要**：本研究利用商业化SMO抗体(克隆号3C1)对基底细胞癌组织进行免疫组化分析，发现SMO蛋白在肿瘤边缘细胞中高表达，且表达水平与患者对vismodegib治疗的敏感性呈负相关，为临床预后提供潜在标志物。
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3. **文献名称**：A Novel Rabbit Polyclonal Antibody for Detecting SMO Mutations in Lung Cancer
**作者**：Rodriguez, M. et al.
**摘要**：报道了一种兔源多克隆SMO抗体的开发与验证，该抗体可识别SMO蛋白的C端突变体(如R562Q)，在非小细胞肺癌组织芯片检测中证实其特异性，为Hedgehog通路异常激活的分子机制研究提供工具。
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4. **文献名称**：Structural Insights into SMO-Ligand Interactions by Surface Plasmon Resonance
**作者**：Wang, Y. et al.
**摘要**：通过表面等离子体共振(SPR)技术，使用重组SMO抗体解析了SMO蛋白与小分子抑制剂(如cyclopamine)的结合动力学，揭示抗体结合可稳定SMO的失活构象，为靶向药物设计提供结构基础。
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提示：实际文献需通过PubMed或Web of Science以关键词“Smoothened antibody”或“SMO inhibitor”检索，并优先选择《Nature》《Cancer Research》等高影响力期刊近5年论文。
**Background of SMO Antibody**
The Smoothened (SMO) antibody targets the SMO protein, a critical component of the Hedgehog (Hh) signaling pathway. SMO is a transmembrane G protein-coupled receptor (GPCR) that regulates cell differentiation, proliferation, and tissue patterning during embryonic development. In the absence of Hh ligands, the pathway is suppressed by the receptor Patched-1 (PTCH1), which inhibits SMO. Upon Hh binding, PTCH1 inhibition is relieved, activating SMO and triggering downstream signaling via GLI transcription factors.
Dysregulation of the Hh pathway, particularly SMO overexpression or activating mutations, is implicated in various cancers, including basal cell carcinoma, medulloblastoma, and pancreatic cancer. SMO antibodies are thus valuable tools for studying Hh pathway mechanisms and developing targeted therapies. Therapeutic SMO inhibitors, such as vismodegib, mimic antibody functions by blocking SMO activity to suppress tumor growth.
In research, SMO antibodies are widely used in techniques like immunohistochemistry, Western blotting, and flow cytometry to detect SMO expression levels, localize the protein in tissues, or assess pathway activation status. They also aid in identifying resistance mechanisms in SMO inhibitor-treated cancers, such as secondary mutations or alternative signaling pathways. Despite clinical promise, challenges like drug resistance and off-target effects highlight the need for continued exploration of SMO-targeting strategies.
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