| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FBL |
| Uniprot No | P22087 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-321aa |
| 氨基酸序列 | MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN |
| 预测分子量 | 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FBL(以Fibrillarin为例)重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**: "Fibrillarin regulates viral RNA-dependent RNA polymerase activity by interacting with the hepatitis C virus NS5B protein"
**作者**: Kim et al.
**摘要**: 研究揭示了FBL蛋白通过重组表达与HCV NS5B聚合酶相互作用，调控病毒RNA复制机制，为抗病毒靶点开发提供依据。
2. **文献名称**: "Structural insights into the role of Fibrillarin in rRNA processing using recombinant protein cryo-EM analysis"
**作者**: Zhou et al.
**摘要**: 通过重组FBL蛋白的冷冻电镜结构解析，阐明其在核糖体RNA甲基化修饰和加工中的分子机制。
3. **文献名称**: "Recombinant expression and functional characterization of Fibrillarin in cancer cell proliferation"
**作者**: Wang et al.
**摘要**: 报道了重组FBL蛋白在多种癌细胞系中的过表达实验，证实其通过调控核仁应激通路促进肿瘤细胞增殖的作用。
注：若FBL指代其他蛋白(如F-box/LRR类)，建议结合具体研究领域补充文献。
**Background of FBL Recombinant Protein**
FBL (F-box/LRR-repeat protein) is a member of the F-box protein family, characterized by an F-box domain that facilitates interactions with Skp1-Cullin1-F-box (SCF) ubiquitin ligase complexes. These complexes play a pivotal role in substrate recognition and protein ubiquitination, a critical process for regulating cellular protein turnover, signaling pathways, and cell cycle progression. The FBL protein also contains leucine-rich repeats (LRRs), which mediate protein-protein interactions, enabling its involvement in diverse biological processes such as immune response modulation, apoptosis, and tumor suppression.
Recombinant FBL protein is engineered through molecular cloning techniques, where the FBL gene is inserted into expression vectors (e.g., bacterial, yeast, or mammalian systems) to produce purified protein for functional studies. Its recombinant form allows researchers to investigate FBL's structural properties, interaction partners, and mechanistic roles in ubiquitination pathways. Notably, dysregulation of FBL has been linked to diseases, including cancers and autoimmune disorders, making it a potential therapeutic target.
The development of recombinant FBL has advanced studies on SCF complex dynamics, substrate specificity, and post-translational regulation. It also serves as a tool for high-throughput screening of ubiquitination inhibitors or stabilizers, contributing to drug discovery. Challenges in production, such as maintaining proper folding and post-translational modifications, are addressed via optimized expression systems and purification strategies. Overall, recombinant FBL protein remains a vital resource for deciphering ubiquitin-proteasome system mechanics and developing targeted therapies.
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