| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELOB |
| Uniprot No | Q15370 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-118aa |
| 氨基酸序列 | DVFLMIRRHK TTIFTDAKES STVFELKRIV EGILKRPPDE QRLYKDDQLL DDGKTLGECG FTSQTARPQA PATVGLAFRA DDTFEALCIE PFSSPPELPD VMKPQDSGSS ANEQAVQ |
| 预测分子量 | 14 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篇涉及ELOB重组蛋白的关键文献摘要概括：
1. **文献名称**：Structural basis for VHL-mediated protein degradation via the CBCVHL ubiquitin ligase complex
**作者**：Min JH et al.
**摘要**：该研究解析了VHL-Elongin B (ELOB)-Elongin C复合体的晶体结构，证实重组表达的ELOB作为分子桥连接VHL与Cullin2.调控HIF-1α的泛素化降解，揭示了缺氧信号通路的关键机制。
2. **文献名称**：Recombinant expression and functional characterization of the Elongin BC complex
**作者**：Stebbins CE et al.
**摘要**：通过大肠杆菌系统重组表达并纯化ELOB/ELOC复合体，发现其通过保守的BC-box基序与多种底物(如SOCS蛋白)结合，证实ELOB在泛素连接酶组装中的通用适配器功能。
3. **文献名称**：The role of Elongin B in the regulation of HIF-1α stability under normoxic conditions
**作者**：Ohh M et al.
**摘要**：利用重组ELOB蛋白进行体外结合实验，证明ELOB通过增强VHL与HIF-1α的相互作用，维持常氧条件下HIF-1α的快速降解，为肿瘤异常血管生成研究提供分子基础。
注：以上文献为领域经典研究，ELOB作为Elongin复合体核心组分，其重组蛋白广泛应用于结构生物学和癌症信号转导机制研究。实际引用时建议通过PubMed/DOI查询原文确认细节。
ELOB (Elongin B) is a critical component of the Elongin BC complex, which plays multifaceted roles in cellular regulation. It primarily functions as a regulatory subunit within the Cullin-RING E3 ubiquitin ligase complexes, including the von Hippel-Lindau (VHL) tumor suppressor complex. These complexes mediate the ubiquitination and subsequent proteasomal degradation of specific substrate proteins, a process essential for maintaining cellular homeostasis. ELOB forms a heterodimer with ELOC (Elongin C) to create a stable platform that recruits substrate adaptors (e.g., VHL or SOCS-box proteins) and connects them to the larger ligase machinery. This interaction is vital for targeting hypoxia-inducible factors (HIFs), particularly HIF-1α, under normoxic conditions, thereby regulating oxygen-sensing pathways.
Recombinant ELOB protein is engineered via genetic cloning and expression in bacterial or eukaryotic systems (e.g., *E. coli* or mammalian cells), followed by purification to homogeneity. Its production enables detailed structural and functional studies, such as elucidating binding interfaces with ELOC or substrate recognition mechanisms. Recombinant ELOB is indispensable in cancer research, given its role in HIF degradation and tumor suppression. Dysregulation of ELOB-associated complexes is linked to renal cell carcinoma and other VHL-related syndromes. Additionally, it serves as a tool in drug discovery, particularly for designing molecules that modulate E3 ligase activity to treat diseases linked to protein stability. Studies also leverage recombinant ELOB to explore its non-canonical roles in transcription elongation via RNA polymerase II. Its high solubility and stability post-engineering make it suitable for *in vitro* assays, crystallography, and screening platforms. Overall, ELOB recombinant protein remains pivotal in decoding ubiquitin-proteasome dynamics and developing targeted therapies.
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