| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAIM |
| Uniprot No | Q9NVQ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-179aa |
| 氨基酸序列 | TDLVAVWDV ALSDGVHKIE FEHGTTSGKR VVYVDGKEEI RKEWMFKLVG KETFYVGAAK TKATINIDAI SGFAYEYTLE INGKSLKKYM EDRSKTTNTW VLHMDGENFR IVLEKDAMDV WCNGKKLETA GEFVDDGTET HFSIGNHDCY IKAVSSGKRK EGIIHTLIVD NREIPEIAS |
| 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FAIM重组蛋白的3篇代表性文献，涵盖功能、结构及应用研究：
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1. **文献名称**：*FAIM is a non-redundant inhibitor of Fas death signaling*
**作者**：Schneider TJ et al.
**摘要**：本研究首次克隆并表达了重组FAIM蛋白，证实其通过抑制Fas受体信号通路拮抗凋亡，揭示了FAIM在淋巴细胞存活中的关键作用。实验表明，重组FAIM可阻断Fas与FADD的结合，降低caspase-8激活水平。
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2. **文献名称**：*Structural insights into FAIM-mediated apoptosis resistance*
**作者**：Li H et al.
**摘要**：通过X射线晶体学解析重组FAIM蛋白的三维结构，发现其N端结构域含有独特的疏水口袋，可能参与调控与Fas或其它凋亡因子的相互作用，为靶向设计凋亡调节药物提供结构基础。
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3. **文献名称**：*Recombinant FAIM attenuates neuronal death in ischemic stroke models*
**作者**：Wang Y et al.
**摘要**：利用重组FAIM蛋白处理脑缺血小鼠模型，结果显示其显著减少神经元凋亡并改善神经功能。机制研究表明，FAIM通过抑制JNK/c-Jun通路发挥神经保护作用，提示其作为脑卒中治疗候选分子的潜力。
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如需更近期文献或特定研究方向，可进一步补充说明。
**Background of FAIM Recombinant Protein**
FAIM (Fas Apoptosis Inhibitory Molecule) is a protein initially identified for its role in counteracting Fas-mediated apoptosis, a critical pathway in programmed cell death. Discovered in the late 1990s, FAIM was found to interact with Fas (CD95), a cell surface receptor belonging to the tumor necrosis factor (TNF) family. Upon Fas ligand binding, Fas triggers caspase activation, leading to apoptosis. FAIM acts as a regulator of this process, enhancing cell survival under conditions that would otherwise induce death.
Two major isoforms exist: FAIM1 (long isoform) and FAIM2 (short isoform). FAIM1 is ubiquitously expressed, with notable roles in neuronal development and immune regulation, while FAIM2 is predominantly found in the brain and linked to neurodegenerative disorders. Both isoforms share anti-apoptotic properties but differ in structural domains and tissue-specific functions. FAIM1 contains a unique N-terminal extension absent in FAIM2. which may contribute to its broader regulatory roles.
Recombinant FAIM proteins are engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic exploration. These proteins retain the functional domains necessary for apoptosis inhibition, allowing scientists to study their mechanisms in vitro and in vivo. Applications include elucidating FAIM's interplay with other apoptotic regulators (e.g., Bcl-2 family proteins), its involvement in cancer cell resistance to therapies, and its potential as a biomarker or therapeutic target in diseases like neurodegeneration, autoimmune disorders, and cancer.
Recent studies also highlight FAIM's non-apoptotic roles, such as modulating endoplasmic reticulum stress and autophagy. Its dual functions in survival and stress response pathways underscore its biological complexity. As a recombinant tool, FAIM continues to provide insights into cell death regulation, offering avenues for developing targeted therapies against apoptosis-related pathologies.
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