| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | Fas-2 |
| Uniprot No | P34082 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-873aa |
| 氨基酸序列 | MGELPPNSVGVFLALLLCSCSLIELTRAQSPILEIYPKQEVQRKPVGKPLILTCRPTVPEPSLVADLQWKDNRNNTILPKPNGRNQPPMYTETLPGESLALMITSLSVEMGGKYYCTASYANTEILEKGVTIKTYVAITWTNAPENQYPTLGQDYVVMCEVKADPNPTIDWLRNGDPIRTTNDKYVVQTNGLLIRNVQESDEGIYTCRAAVIETGELLERTIRVEVFIQPEIISLPTNLEAVEGKPFAANCTARGKPVPEISWIRDATQLNVATADRFQVNPQTGLVTISSVSQDDYGTYTCLAKNRAGVVDQKTKLNVLVRPQIYELYNVTGARTKEIAITCRAKGRPAPAITFRRWGTQEEYTNGQQDDDPRIILEPNFDEERGESTGTLRISNAERSDDGLYQCIARNKGADAYKTGHITVEFAPDFSHMKELPPVFSWEQRKANLSCLAMGIPNATIEWHWNGRKIKDLYDTNLKIVGTGPRSDLIVHPVTRQYYSGYKCIATNIHGTAEHDMQLKEARVPDFVSEAKPSQLTATTMTFDIRGPSTELGLPILAYSVQYKEALNPDWSTAYNRSWSPDSPYIVEGLRPQTEYSFRFAARNQVGLGNWGVNQQQSTPRRSAPEEPKPLHNPVQHDKEEPVVVSPYSDHFELRWGVPADNGEPIDRYQIKYCPGVKISGTWTELENSCNTVEVMETTSFEMTQLVGNTYYRIELKAHNAIGYSSPASIIMKTTRGIDVIQVAERQVFSSAAIVGIAIGGVLLLLFVVDLLCCITVHMGVMATMCRKAKRSPSEIDDEAKLGSGQLVKEPPPSPLPLPPPVKLGGSPMSTPLDEKEPLRTPTGSIKQNSTIEFDGRFVHSRSGEIIGKNSAV |
| 预测分子量 | 96,9 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Fas-2重组蛋白的3篇参考文献概览(注：Fas-2在不同研究领域可能有不同定义，以下假设聚焦于病原体相关蛋白的研究)：
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1. **文献名称**: *"Expression and functional characterization of Streptococcus suis Fas-2 recombinant protein in bacterial adhesion"*
**作者**: Zhang Y, et al.
**摘要**: 本研究克隆并表达猪链球菌Fas-2蛋白，发现重组蛋白显著增强细菌对宿主上皮细胞的黏附能力，提示其在感染初期的重要作用。
2. **文献名称**: *"Recombinant Fas-2 protein as a potential vaccine candidate against Leishmania infection"*
**作者**: Gupta S, et al.
**摘要**: 通过大肠杆菌系统表达利什曼原虫Fas-2表面抗原，动物实验表明该重组蛋白可诱导Th1免疫反应，显著降低寄生虫负荷，具有疫苗开发潜力。
3. **文献名称**: *"Structural analysis of Fas-2 adhesin from Candida albicans reveals glycosylation-dependent binding mechanisms"*
**作者**: Li H, et al.
**摘要**: 利用重组Fas-2蛋白解析其晶体结构，发现糖基化修饰影响其与宿主细胞表面受体互作，为抗真菌药物设计提供新靶点。
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**说明**：
- 以上文献为示例，实际研究中需根据具体物种(如链球菌、真菌等)检索真实文献。
- 若需精准引用，建议通过PubMed或Google Scholar以“Fas-2 recombinant protein”+研究领域(如“Streptococcus”“vaccine”)为关键词筛选。
**Background of Fas-2 Recombinant Protein**
The Fas-2 recombinant protein is a engineered form of the Fas ligand (FasL), a critical member of the tumor necrosis factor (TNF) superfamily. FasL plays a pivotal role in regulating programmed cell death (apoptosis) by binding to its cognate receptor, Fas (CD95/APO-1), on target cells. This interaction triggers the formation of the death-inducing signaling complex (DISC), activating caspases and downstream apoptotic pathways. FasL exists in both membrane-bound and soluble forms, with the latter generated via metalloproteinase-mediated cleavage. Dysregulation of the Fas/FasL system is implicated in immune homeostasis, autoimmune disorders, cancer immune evasion, and neurodegenerative diseases.
Recombinant Fas-2 protein is typically produced using *in vitro* expression systems, such as *E. coli* or mammalian cell cultures, to ensure high purity and bioactivity. Advanced techniques like affinity tagging (e.g., His-tag) facilitate efficient purification, while structural modifications (e.g., truncations or fusion proteins) may enhance stability or specificity. Quality control assays, including SDS-PAGE, Western blot, and functional apoptosis assays, validate its integrity and activity.
As a research tool, Fas-2 recombinant protein is widely used to study apoptotic mechanisms, screen therapeutic agents targeting the Fas pathway, and model diseases linked to aberrant cell survival. In therapeutic contexts, it holds potential for cancer immunotherapy by selectively inducing apoptosis in malignant cells, though challenges like off-target toxicity and resistance mechanisms remain. Additionally, it serves as a reagent in *in vitro* T-cell cytotoxicity assays and immune tolerance studies. Ongoing research explores engineered variants with improved pharmacokinetics or targeted delivery systems to maximize clinical efficacy.
In summary, Fas-2 recombinant protein bridges fundamental apoptosis research and translational applications, offering insights into cell death regulation and opportunities for novel treatments in oncology and immunology.
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