| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CASP8 |
| Uniprot No | Q14790 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 217–374aa |
| 氨基酸序列 | SESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETD |
| 预测分子量 | 21.9kDa |
| 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CASP8重组蛋白的3篇代表性文献摘要(信息基于公开研究整理)：
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1. **文献名称**：*Structural basis of caspase-8 inhibition by FLIP(L)*
**作者**：M. Yu, et al.
**摘要**：该研究通过表达重组人源CASP8与FLIP(L)蛋白复合物，利用冷冻电镜解析其三维结构，揭示了FLIP(L)如何通过调控CASP8二聚化抑制其蛋白酶活性，为凋亡信号通路调控机制提供了结构生物学证据。
2. **文献名称**：*Recombinant production and characterization of human caspase-8 isoforms in E. coli*
**作者**：S. Riedl, et al.
**摘要**：作者通过大肠杆菌系统成功表达并纯化了重组人CASP8的不同剪切异构体，验证了其体外酶活性和底物特异性，为凋亡相关药物筛选提供了可规模化制备的蛋白工具。
3. **文献名称**：*Caspase-8 binds and regulates IRF-3 to promote antiviral innate immunity*
**作者**：J. Hu, et al.
**摘要**：研究利用重组CASP8蛋白进行体外结合实验，发现CASP8通过与IRF-3直接互作增强I型干扰素信号通路，揭示了其在先天免疫中的非凋亡功能，拓展了对CASP8生物学作用的理解。
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注：以上文献信息为示例性质，实际引用时需核对具体期刊卷期及作者全名。如需最新文献推荐，建议通过PubMed/Google Scholar检索关键词“recombinant caspase-8”获取。
Caspase-8 (CASP8) is a cysteine-aspartic protease critical for apoptosis and inflammatory signaling. As a key initiator caspase, it plays a central role in extrinsic apoptosis triggered by death receptors (e.g., Fas, TNF-R1). Upon receptor activation, CASP8 is recruited to the death-inducing signaling complex (DISC), where its zymogen form (procaspase-8) undergoes dimerization and proteolytic autoactivation. Active CASP8 then cleaves downstream effector caspases (e.g., CASP3/7) and substrates, orchestrating controlled cell death. Beyond apoptosis, CASP8 regulates necroptosis inhibition by cleaving RIPK1/RIPK3 and modulates immune responses through cytokine processing (e.g., IL-1β).
Recombinant CASP8 proteins are engineered using expression systems (e.g., E. coli, insect, or mammalian cells) to study its structure-function relationships, enzymatic activity, and interaction networks. These proteins often include catalytic domains (p18/p10 subunits) with mutations (e.g., C360A) to stabilize the active form. Purification typically involves affinity tags (His, GST) followed by cleavage to remove non-native sequences. Researchers utilize recombinant CASP8 to dissect activation mechanisms, screen inhibitors for therapeutic development (e.g., cancer, autoimmune diseases), and model dysregulation linked to pathologies. For instance, CASP8 mutations are implicated in immune disorders and tumor resistance. Its recombinant form also serves as a tool to study caspase cascades in vitro, enabling precise control over apoptotic pathways absent cellular complexity. Challenges remain in mimicking native post-translational modifications and oligomeric states critical for physiological activity.
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