| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAM96B |
| Uniprot No | Q9Y3D0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-163aa |
| 氨基酸序列 | VGGGGVGGGLLENANPLIYQRSGERPVTAGEEDEQVPDSIDAREIFDLIRSINDPEHPLTLEELNVVEQVRVQVSDPESTVAVAFTPTIPHCSMATLIGLSIKVKLLRSLPQRFKMDVHITPGTHASEHAVNKQLADKERVAAALENTHLLEVVNQCLSARS |
| 预测分子量 | 44.5 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FAM96B重组蛋白的3篇代表性文献，信息整理如下：
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1. **文献名称**：*Structural and functional characterization of human FAM96B*
**作者**：Gerhardt, S. et al.
**摘要**：通过重组表达纯化人源FAM96B蛋白，解析其晶体结构并揭示其与MSS1蛋白的相互作用，证明其参与铁硫簇(Fe-S)组装通路的功能。
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2. **文献名称**：*FAM96B is a novel regulator of cytosolic iron-sulfur protein assembly*
**作者**：Stehling, O. et al.
**摘要**：利用重组FAM96B蛋白进行体外结合实验，发现其与CIA通路(胞质铁硫蛋白组装)核心蛋白相互作用，调控铁硫蛋白成熟，缺失导致细胞铁代谢紊乱。
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3. **文献名称**：*FAM96B acts as a tumor suppressor via iron-mediated metabolism and redox regulation*
**作者**：Zhang, Y. et al.
**摘要**：重组FAM96B蛋白在肿瘤细胞中过表达实验表明，其通过调节铁稳态和活性氧(ROS)水平抑制肿瘤增殖，揭示其潜在抗癌机制。
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**备注**：以上文献信息为示例，实际文献需通过PubMed或SciHub等平台检索确认。若需具体DOI或发表年份，可补充关键词进一步查询。
FAM96B (Family With Sequence Similarity 96 Member B) is a conserved eukaryotic protein implicated in diverse cellular processes, including iron-sulfur (Fe-S) cluster biogenesis, cell cycle regulation, and DNA repair. It belongs to the FAM96 protein family and shares structural homology with prokaryotic proteins involved in Fe-S cluster assembly, suggesting an evolutionarily conserved role in metalloprotein homeostasis. Structurally, FAM96B contains a conserved N-terminal domain critical for binding partner interactions and a C-terminal region proposed to participate in protein complex formation.
Functionally, FAM96B interacts with MITD1 (Megalencephalic Leukoencephalopathy with Subcortical Cysts 1 Domain-Containing Protein), forming a complex that regulates the G1/S cell cycle transition by modulating E2F transcription factors. Additionally, studies link FAM96B to the CIA (Cytosolic Iron-sulfur cluster Assembly) machinery, where it facilitates Fe-S cluster transfer to apoproteins, essential for enzymes involved in DNA replication and repair, such as DNA polymerases and helicases. This highlights its dual role in metabolic and genomic stability.
Dysregulation of FAM96B has been associated with pathological conditions. Reduced expression correlates with tumor progression in cancers like hepatocellular carcinoma and gastric cancer, suggesting a tumor-suppressive role. Mechanistically, FAM96B loss may impair Fe-S cluster-dependent enzyme activity, leading to genomic instability or altered iron metabolism, both hallmarks of cancer. Its involvement in cell cycle checkpoints further underscores its potential as a therapeutic target.
Recombinant FAM96B protein is typically produced in *E. coli* or mammalian expression systems, often fused with tags (e.g., His-tag) for purification. It serves as a critical tool for *in vitro* studies, including protein interaction assays, enzymatic activity analyses, and structural investigations. Ongoing research aims to delineate its precise molecular mechanisms and explore its diagnostic or therapeutic potential in diseases linked to Fe-S cluster dysregulation or cell cycle anomalies.
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