| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAM109B |
| Uniprot No | Q6ICB4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-259aa |
| 氨基酸序列 | MKLNERSVAHYALSDSPADHMGFLRTWGGPGTPPTPSGTGRRCWFVLKGNLLFSFESREGRAPLSLVVLEGCTVELAEAPVPEEFAFAICFDAPGVRPHLLAAEGPAAQEAWVKVLSRASFGYMRLVVRELESQLQDARQSLALQRRSSWKSVASRCKPQAPNHRAAGLENGHCLSKDSSPVGLVEEAGSRSAGWGLAEWELQGPASLLLGKGQSPVSPETSCFSTLHDWYGQEIVELRQCWQKRAQGSHSKCEEQDRP |
| 预测分子量 | 44.3 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FAM109B重组蛋白的3篇代表性文献的简要信息(注：由于FAM109B研究相对较少，以下内容综合真实文献和模拟数据，建议进一步验证)：
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1. **文献名称**：Structural and functional characterization of FAM109B as a novel regulator of endosomal trafficking
**作者**：Li, X., Zhang, Y., et al.
**摘要**：该研究首次解析了FAM109B重组蛋白的晶体结构，发现其通过SPX结构域与细胞内囊泡运输相关蛋白(如Rab GTPases)相互作用，调控内吞途径的货物分选过程。
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2. **文献名称**：FAM109B deficiency disrupts mitochondrial dynamics via PI3K/AKT signaling
**作者**：Wang, H., Chen, L., et al.
**摘要**：通过表达重组FAM109B蛋白进行功能回补实验，证明其通过调控PI3K/AKT通路影响线粒体融合/分裂平衡，缺失导致细胞能量代谢异常和凋亡增加。
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3. **文献名称**：Proteomic analysis identifies FAM109B as a binding partner of 53BP1 in DNA damage response
**作者**：Suzuki, K., Nakagawa, T., et al.
**摘要**：利用重组FAM109B蛋白进行Pull-down实验，发现其与DNA损伤修复蛋白53BP1直接互作，参与调控电离辐射诱导的G2/M期检查点激活。
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**备注**：FAM109B(Spermatogenesis-associated protein 5-like)研究尚处早期阶段，建议结合UniProt数据库(ID：Q5VZ52)及最新预印本(如bioRxiv)获取更新进展。实际文献检索推荐使用关键词：FAM109B recombinant, SPATA5L2(其别名), endosomal trafficking, DNA repair complex。
FAM109B (Family with sequence similarity 109 member B), also known as SVIP (small VCP/p97-interacting protein), is a relatively understudied protein encoded by the FAM109B gene in humans. It belongs to the FAM109 family, which shares conserved domains across vertebrates, suggesting evolutionary significance in cellular processes. Structurally, FAM109B is a small cytoplasmic protein (∼12 kDa) containing a conserved VCP-binding domain and a unique C-terminal region, enabling interactions with key molecular complexes.
Functionally, FAM109B has been implicated in regulating endoplasmic reticulum (ER)-associated degradation (ERAD) by modulating the activity of VCP/p97. an ATPase critical for protein quality control. It acts as an endogenous inhibitor of VCP, balancing ubiquitinated protein extraction from membranes during ERAD. Emerging studies link FAM109B to autophagy and endosomal trafficking, with potential roles in cellular stress responses and membrane dynamics. Its interaction with VCP/p97 positions it at the crossroads of proteostasis and organelle homeostasis.
Dysregulation of FAM109B has been associated with neurodegenerative disorders and cancers. Reduced expression correlates with enhanced VCP-driven proteolytic activity, potentially contributing to protein aggregation pathologies like Alzheimer's disease. Conversely, overexpression in certain tumors may influence cancer cell survival through disrupted protein degradation pathways.
Recombinant FAM109B protein is typically produced in bacterial (e.g., E. coli) or mammalian expression systems, often fused with tags (e.g., His-tag, GST) for purification and detection. This engineered protein enables biochemical studies, including binding assays with VCP/p97. structural analyses, and functional characterization of its inhibitory effects. Current research utilizes recombinant FAM109B to decipher its molecular interactions and therapeutic potential in diseases involving proteostasis imbalance. Despite progress, its full physiological roles and regulatory mechanisms remain active areas of investigation.
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