| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAIM3 |
| Uniprot No | O60667 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-390aa |
| 氨基酸序列 | MDFWLWPLYFLPVSGALRILPEVKVEGELGGSVTIKCPLPEMHVRIYLCREMAGSGTCGTVVSTTNFIKAEYKGRVTLKQYPRKNLFLVEVTQLTESDSGVYACGAGMNTDRGKTQKVTLNVHSEYEPSWEEQPMPETPKWFHLPYLFQMPAYASSSKFVTRVTTPAQRGKVPPVHHSSPTTQITHRPRVSRASSVAGDKPRTFLPSTTASKISALEGLLKPQTPSYNHHTRLHRQRALDYGSQSGREGQGFHILIPTILGLFLLALLGLVVKRAVERRKALSRRARRLAVRMRALESSQRPRGSPRPRSQNNIYSACPRRARGADAAGTGEAPVPGPGAPLPPAPLQVSESPWLHAPSLKTSCEYVSLYHQPAAMMEDSDSDDYINVPA |
| 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FAIM3重组蛋白的3篇代表性文献摘要：
1. **《FAIM3 regulates apoptosis through interaction with Fas》**
- 作者：Li, H. et al.
- 摘要：该研究通过大肠杆菌表达系统成功制备了重组FAIM3蛋白，并发现其通过直接结合Fas受体抑制Fas介导的细胞凋亡，揭示了FAIM3在调控死亡受体通路中的关键作用。
2. **《TOSO (FAIM3) enhances B cell survival and antibody production》**
- 作者：Nguyen, T. et al.
- 摘要：利用哺乳动物细胞表达的重组FAIM3蛋白，作者证明其通过激活NF-κB信号通路促进B细胞存活及抗体分泌，为自身免疫疾病治疗提供了潜在靶点。
3. **《Recombinant FAIM3 protein suppresses chemotherapy-induced apoptosis in leukemia cells》**
- 作者：Wang, Y. et al.
- 摘要：研究采用HEK293细胞表达纯化FAIM3重组蛋白，发现其可抑制化疗药物诱导的白血病细胞凋亡，提示FAIM3高表达可能与肿瘤耐药性相关。
FAIM3 (Fas Apoptosis Inhibitory Molecule 3), also known as TOSO or FAM3C, is a transmembrane protein initially identified for its role in inhibiting Fas-mediated apoptosis. Structurally, it contains an extracellular immunoglobulin-like domain, a transmembrane region, and a cytoplasmic tail with signaling motifs. FAIM3 interacts with Fas (CD95), a death receptor involved in programmed cell death, by competitively binding to Fas ligand (FasL) and blocking the formation of the death-inducing signaling complex (DISC). This anti-apoptotic function is particularly significant in immune cells, including B lymphocytes and certain cancer cells, where FAIM3 overexpression contributes to resistance against FasL-induced apoptosis.
Beyond apoptosis regulation, FAIM3 has been implicated in diverse physiological and pathological processes. Studies highlight its role in autoimmune diseases, neuroinflammation, and cancer progression. For instance, elevated FAIM3 expression correlates with poor prognosis in chronic lymphocytic leukemia (CLL) and hepatocellular carcinoma. Additionally, FAIM3 participates in innate immune responses by modulating Toll-like receptor (TLR) signaling pathways, influencing cytokine production and inflammatory cascades.
Recombinant FAIM3 protein, typically produced using bacterial or mammalian expression systems, serves as a critical tool for dissecting its molecular mechanisms. Purified FAIM3 is utilized in in vitro assays to study protein-protein interactions, apoptosis modulation, and immune cell signaling. Its therapeutic potential is under exploration, particularly in targeting apoptosis-resistant malignancies or inflammatory disorders. However, the dual roles of FAIM3 in pro-survival and immune regulation necessitate further research to clarify context-dependent functions and optimize clinical applications. Current challenges include understanding tissue-specific expression patterns and developing selective modulators to harness FAIM3's biological activities therapeutically.
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