| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPOP |
| Uniprot No | O43791 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-374aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSRVPSPPPPAEMSSGPVAESWCYTQIKVV KFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEES KDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKD WGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVK VPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFE HEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKY ALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHAS DVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS |
| 预测分子量 | 44 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3篇关于SPOP重组蛋白研究的参考文献概览：
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1. **文献名称**：*Structural basis of phosphodiester bond recognition by SPOP in the non-canonical BMP signaling pathway*
**作者**：Zhuang M. et al. (Cell Research, 2014)
**摘要**：通过X射线晶体学解析了SPOP蛋白与其底物(磷酸二酯酶PDEδ)的复合物结构，揭示了SPOP通过MATH结构域特异性识别底物的分子机制，为SPOP介导的泛素化调控提供了结构基础。
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2. **文献名称**：*Cancer-associated mutations in SPOP disrupt its ability to target androgen receptor for degradation*
**作者**：Gan W. et al. (Nature Communications, 2015)
**摘要**：研究发现前列腺癌中SPOP的突变(如Y87N、F133V)会破坏其与雄激素受体(AR)的结合，导致AR蛋白异常积累，促进肿瘤生长，揭示了SPOP突变致癌的分子机制。
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3. **文献名称**：*SPOP regulates prostate epithelial cell proliferation and promotes ubiquitination-mediated turnover of oncogenic protein DEK*
**作者**：Zhang J. et al. (Oncogene, 2017)
**摘要**：利用重组SPOP蛋白进行功能实验，证明其通过泛素化降解致癌蛋白DEK，抑制前列腺上皮细胞增殖，并发现SPOP缺失会促进前列腺癌进展。
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**注**：以上文献均聚焦于SPOP的结构功能及病理机制研究，涉及重组蛋白在泛素化调控、癌症突变效应等领域的应用。如需具体DOI或补充文献，可进一步提供方向。
SPOP (Speckle-type POZ Protein) is a critical adaptor protein in the CUL3-RING ubiquitin ligase (CRL3) complex, playing a central role in substrate recognition and proteasomal degradation. It contains two functional domains: an N-terminal MATH (meprin and TRAF homology) domain for binding substrates and a C-terminal BTB (Broad-complex, Tramtrack, and Bric-à-brac) domain that mediates interaction with CUL3. SPOP selectively recruits substrates via conserved SPOP-binding motifs (SBMs), tagging them with ubiquitin for degradation. This regulatory mechanism influences diverse cellular processes, including signal transduction (Hedgehog, Wnt, Hippo pathways), chromatin remodeling, apoptosis, and cell cycle control.
SPOP is notable for its involvement in cancer. Recurrent mutations in SPOP, particularly in prostate and endometrial cancers, disrupt substrate binding, leading to aberrant stabilization of oncoproteins like AR, ERG, and BET proteins. These mutations are often linked to tumor progression and therapeutic resistance. Conversely, SPOP’s tumor-suppressive role in other contexts involves degrading oncogenic substrates such as DAXX and TRIM24. Beyond cancer, SPOP regulates developmental pathways, as evidenced by its requirement for organogenesis in model organisms.
The structural basis of SPOP-substrate interactions has been extensively studied, revealing how disease-associated mutations impair substrate recognition. Its dual role as both oncogene and tumor suppressor, depending on cellular context, makes SPOP a compelling therapeutic target. Current research focuses on developing small molecules to modulate SPOP activity or restore function in mutation-driven cancers, highlighting its significance in precision oncology and disease biology.
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