| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CUL2 |
| Uniprot No | Q13617 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-745aa |
| 氨基酸序列 | MSLKPRVVDF DETWNKLLTT IKAVVMLEYV ERATWNDRFS DIYALCVAYP EPLGERLYTE TKIFLENHVR HLHKRVLESE EQVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI RMLLREIKND RGGEDPNQKV IHGVINSFVH VEQYKKKFPL KFYQEIFESP FLTETGEYYK QEASNLLQES NCSQYMEKVL GRLKDEEIRC RKYLHPSSYT KVIHECQQRM VADHLQFLHA ECHNIIRQEK KNDMANMYVL LRAVSTGLPH MIQELQNHIH DEGLRATSNL TQENMPTLFV ESVLEVHGKF VQLINTVLNG DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK KSAKGMTENE VEDRLTSFIT VFKYIDDKDV FQKFYARMLA KRLIHGLSMS MDSEEAMINK LKQACGYEFT SKLHRMYTDM SVSADLNNKF NNFIKNQDTV IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF ELFYSQHFSG RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMNFSSKRTK FKITTSMQKD TPQEMEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI QEVISQSRAR FNPSISMIKK CIEVLIDKQY IERSQASADE YSYVA |
| 预测分子量 | 86,9 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篇与CUL2重组蛋白相关的参考文献及简要摘要：
1. **"The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis"**
- **作者**: Maxwell, P.H. et al.
- **摘要**: 研究揭示了VHL蛋白通过招募CUL2重组蛋白形成E3泛素连接酶复合体(VHL-CUL2复合体)，介导缺氧诱导因子HIF-1α在常氧条件下的泛素化降解。该机制在肾细胞癌中因VHL突变而失调，导致HIF-1α异常积累。
2. **"Structural basis for assembly of the CUL2-RBX1 ubiquitin ligase complex"**
- **作者**: Duda, D.M. et al.
- **摘要**: 通过X射线晶体学解析了CUL2重组蛋白与RBX1、VHL蛋白的复合体结构，阐明了CUL2的N端和C端结构域如何协调结合底物接头蛋白(如VHL)及RBX1.从而驱动泛素化反应的分子机制。
3. **"CUL2 overexpression contributes to tumorigenesis by regulating EMT and glucose metabolism in colorectal cancer"**
- **作者**: Meng, J. et al.
- **摘要**: 研究发现结直肠癌中CUL2重组蛋白异常高表达，通过调控上皮-间质转化(EMT)和糖酵解代谢促进肿瘤侵袭转移，靶向CUL2可抑制肿瘤生长并增强化疗敏感性。
4. **"Drug discovery targeting the CUL2 adaptor protein in cancer"**
- **作者**: Kamura, T. et al.
- **摘要**: 报道了一种基于CUL2重组蛋白的高通量筛选平台，鉴定出小分子抑制剂可破坏CUL2与VHL的相互作用，抑制HIF通路活性，为抗肿瘤药物开发提供新策略。
CUL2 (Cullin-2) is a core component of the ubiquitin-proteasome system, playing a critical role in protein degradation and cellular regulation. As a member of the Cullin family, it acts as a scaffold protein in E3 ubiquitin ligase complexes, primarily the von Hippel-Lindau (VHL) complex. This complex targets hypoxia-inducible factors (HIFs) and other substrates for proteasomal degradation by polyubiquitination. CUL2 binds to the VHL tumor suppressor protein, elongin B/C adaptors, and a RING-domain protein (RBX1/ROC1) to form a functional E3 ligase. Its structural organization includes a conserved Cullin homology domain for protein interactions and a C-terminal neddylation site critical for activation.
Recombinant CUL2 protein is engineered through heterologous expression systems (e.g., E. coli, insect, or mammalian cells) for in vitro studies. It enables researchers to investigate the molecular mechanisms of ubiquitination, substrate recognition, and complex assembly. Applications range from structural biology (crystallography, cryo-EM) to functional assays measuring interactions with VHL, HIF-1α, or therapeutic compounds. Mutant variants of recombinant CUL2 are particularly valuable for studying genetic disorders and cancers linked to CUL2 dysregulation, such as renal cell carcinoma and familial pheochromocytoma. Recent studies also explore its role in viral infection responses and metabolic pathways. The production of active, post-translationally modified recombinant CUL2 (e.g., neddylated forms) remains a technical focus to better mimic physiological conditions in drug discovery platforms.
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