| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMO |
| Uniprot No | Q99835 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-787aa |
| 氨基酸序列 | MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF |
| 预测分子量 | 86,3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于SMO(Smoothened)重组蛋白的示例参考文献(仅供参考，实际引用需核对原文)：
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1. **"Structural Basis of Smoothened Activation in Hedgehog Signaling"**
*By Byrne EFX et al. (2018)*
摘要：通过冷冻电镜解析SMO重组蛋白的激活态结构，揭示其与胆固醇类似物的结合机制，为Hedgehog信号通路中SMO的构象变化提供分子基础。
2. **"Recombinant Expression and Purification of Human Smoothened for Drug Discovery"**
*By Wang C et al. (2016)*
摘要：开发了一种高效表达和纯化人源SMO重组蛋白的方法，用于高通量药物筛选，并验证其在拮抗剂结合实验中的功能性应用。
3. **"Mechanism of Smoothened Regulation by Its Extracellular Domains"**
*By Zhang X et al. (2020)*
摘要：研究SMO重组蛋白的胞外结构域对其活性的调控作用，发现特定区域在配体识别和信号转导中的关键功能，为靶向治疗提供新策略。
4. **"Targeting Oncogenic Smoothened with Recombinant Antibodies"**
*By Li Y et al. (2019)*
摘要：利用重组SMO蛋白筛选出特异性单克隆抗体，抑制Hedgehog通路异常激活，在肿瘤模型中显示抗增殖效果。
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注：以上文献信息为示例，实际研究中请通过PubMed、Web of Science等平台检索具体文献并核实细节。
**Background of SMO Recombinant Protein**
The Smoothened (SMO) protein is a critical component of the Hedgehog (Hh) signaling pathway, an evolutionarily conserved system essential for embryonic development, tissue homeostasis, and cell proliferation regulation. SMO functions as a G protein-coupled receptor (GPCR) localized on the cell membrane. In the absence of Hh ligands, the pathway remains inactive, but upon ligand binding to the receptor Patched (PTCH1), SMO is relieved from suppression, triggering downstream transcriptional activation via GLI transcription factors. Dysregulation of SMO is implicated in various cancers, including basal cell carcinoma and medulloblastoma, making it a therapeutic target.
Recombinant SMO proteins are engineered using biotechnological methods, such as expression in mammalian or insect cell systems, to produce purified, functional SMO for research and drug development. These proteins retain key structural features, including seven transmembrane domains and extracellular loops critical for ligand interactions. Recombinant SMO enables detailed studies of its activation mechanisms, interactions with inhibitors (e.g., vismodegib), and structural analysis via crystallography.
In cancer research, SMO recombinant proteins aid in screening antitumor compounds and understanding resistance mechanisms. They also support antibody development for diagnostic or therapeutic purposes. Furthermore, recombinant SMO serves as a tool to explore non-canonical signaling roles in diseases beyond cancer, such as fibrosis and neurodegenerative disorders. Despite progress, challenges remain in mimicking native post-translational modifications and membrane-associated behaviors in vitro. Advances in protein engineering and structural biology continue to refine SMO recombinant tools, enhancing their utility in both basic science and translational applications.
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