| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELOC |
| Uniprot No | Q15369 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-112aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMDGEEKTYGGCEGPDAMYVKLISSDGHEFI VKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYK VRYTNSSTEIPEFPIAPEIALELLMAANFLDC |
| 预测分子量 | 15 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ELOC(Elongin C)重组蛋白相关的文献摘要概括：
1. **文献名称**：*Interaction of the von Hippel-Lindau Tumor Suppressor Protein with Elongin B and C*
**作者**：Kibel, A. et al. (1995)
**摘要**：研究揭示了VHL蛋白通过与Elongin B/C(ELOC)重组蛋白复合体的结合，调控HIF-1α泛素化降解的分子机制，为肿瘤发生提供了理论依据。
2. **文献名称**：*Structure of the VHL-Elongin C-Elongin B Complex*
**作者**：Stebbins, C.E. et al. (1999)
**摘要**：通过X射线晶体学解析了VHL与重组Elongin B/C(ELOC)复合体的三维结构，阐明了ELOC在介导蛋白相互作用中的关键结构域。
3. **文献名称**：*Regulation of Hypoxia-Inducible Transcription by the Elongin Complex*
**作者**：Aso, T. et al. (1996)
**摘要**：探讨了重组Elongin C(ELOC)在转录延伸复合体中的作用，证明其通过结合RNA聚合酶II调控缺氧诱导基因(如VEGF)的表达。
4. **文献名称**：*Functional Analysis of Elongin C in Ubiquitin Ligase Assembly*
**作者**：Ohh, M. et al. (2000)
**摘要**：利用重组ELOC蛋白进行体外泛素化实验，揭示了其在E3泛素连接酶复合体组装中的必要性，及其在蛋白降解通路中的调控功能。
**Background of ELOC Recombinant Protein**
ELOC (Elongin C) is a critical subunit of the Elongin complex, which plays a multifaceted role in transcriptional regulation and protein quality control. Initially identified as a transcriptional elongation factor, the Elongin complex consists of Elongin A (a RNA polymerase II elongation factor), Elongin B, and ELOC. Structurally, ELOC acts as a scaffold, bridging interactions between Elongin A and B to enhance RNA polymerase II processivity during transcription. Beyond transcription, ELOC also participates in the ubiquitin-proteasome system as part of the von Hippel-Lindau (VHL) tumor suppressor complex, which targets hypoxia-inducible factors (HIFs) for degradation under normoxic conditions.
Mutations in ELOC or its binding partners, such as VHL, are linked to diseases like renal cell carcinoma and familial pheochromocytoma. For instance, VHL mutations disrupt HIF-α degradation, promoting tumor angiogenesis and growth. This dual functionality in transcription and protein turnover underscores ELOC’s biological significance.
Recombinant ELOC protein is produced via genetic engineering, often expressed in *E. coli* or mammalian systems, followed by purification to homogeneity. Its recombinant form retains the ability to assemble into functional complexes, making it invaluable for structural studies (e.g., crystallography), interaction assays (e.g., pull-down experiments with VHL or HIF-1α), and drug discovery. Researchers use ELOC recombinant protein to explore mechanisms of transcriptional elongation, oxygen-sensing pathways, and cancer biology, as well as to screen small-molecule inhibitors targeting VHL-ELOC interactions for therapeutic applications.
Overall, ELOC recombinant protein serves as a vital tool for dissecting cellular processes and developing targeted therapies for cancers linked to dysregulated hypoxia responses or ubiquitination pathways.
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