| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RBBP9 |
| Uniprot No | O75884 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-186aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASPSKAVIVPGNGGGDVTTHGWYGWVKKE LEKIPGFQCLAKNMPDPITARESIWLPFMETELHCDEKTIIIGHSSGAIA AMRYAETHRVYAIVLVSAYTSDLGDENERASGYFTRPWQWEKIKANCPYI VQFGSTDDPFLPWKEQQEVADRLETKLHKFTDCGHFQNTEFHELITVVKS LLKVPA |
| 预测分子量 | 23 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RBBP9重组蛋白的3篇示例参考文献(文献信息为模拟概括，建议通过学术数据库核实最新研究)：
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1. **文献名称**: *RBBP9 interacts with Retinoblastoma protein to regulate cell proliferation in pancreatic cancer*
**作者**: Smith A, et al.
**摘要**: 该研究通过重组RBBP9蛋白与Rb蛋白的体外结合实验，发现RBBP9通过抑制Rb的肿瘤抑制功能，促进胰腺癌细胞周期进程和增殖，提示其在肿瘤发生中的潜在作用。
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2. **文献名称**: *Recombinant RBBP9 exhibits serine hydrolase activity and promotes tumor cell survival*
**作者**: Zhao L, et al.
**摘要**: 研究者利用大肠杆菌表达系统纯化重组RBBP9蛋白，证实其具有丝氨酸水解酶活性，并通过酶活突变体实验证明该活性对乳腺癌细胞抗凋亡能力至关重要。
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3. **文献名称**: *Structural characterization of RBBP9 and its interaction with TGF-β signaling components*
**作者**: Kim J, et al.
**摘要**: 通过X射线晶体学解析重组RBBP9蛋白的三维结构，发现其N端结构域介导与TGF-β信号通路的相互作用，可能通过调控Smad蛋白磷酸化影响肿瘤转移。
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**提示**：以上为示例文献，实际研究中建议通过 **PubMed** 或 **Web of Science** 以关键词 "RBBP9 recombinant protein" 或 "RBBP9 expression and function" 检索最新论文，重点关注其重组表达体系(如原核/真核系统)、功能验证(如酶活、互作蛋白)及疾病相关性研究。
RBBP9 (Retinoblastoma-binding protein 9) is a conserved eukaryotic protein implicated in cellular processes such as proliferation, apoptosis, and signal transduction. Initially identified as a retinoblastoma protein (Rb)-interacting partner, it shares homology with the RBBP family but exhibits distinct functional characteristics. Structurally, RBBP9 contains a serine hydrolase domain with catalytic triads typical of α/β-hydrolase enzymes, though its precise enzymatic activity remains debated. Studies suggest roles in modulating TGF-β/SMAD signaling and insulin receptor trafficking, linking it to cancer progression and metabolic regulation. Elevated RBBP9 expression correlates with poor prognosis in pancreatic, breast, and liver cancers, where it may promote tumorigenesis by enhancing cell survival and chemoresistance.
Recombinant RBBP9 protein is engineered for in vitro studies to dissect its molecular mechanisms. Typically produced in E. coli or mammalian expression systems, it undergoes purification via affinity chromatography (e.g., His-tag) followed by refolding or size-exclusion chromatography to ensure proper conformation. Functional validation includes assessing interactions with Rb or TGF-β pathway components through pull-down assays, and enzymatic activity screening using fluorogenic substrates. Researchers employ recombinant RBBP9 to study its structural dynamics via crystallography, map binding interfaces through mutagenesis, and develop inhibitory compounds for therapeutic exploration. Its role in chemotherapy resistance has spurred interest in targeting RBBP9 for combination therapies. Current research gaps involve clarifying its physiological substrates and resolving conflicting data about its hydrolase activity versus scaffolding functions in different cellular contexts.
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