| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CASP6 |
| Uniprot No | P55212 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-179aa |
| 氨基酸序列 | AFYKREM FDPAEKYKMD HRRRGIALIF NHERFFWHLT LPERRGTCAD RDNLTRRFSD LGFEVKCFND LKAEELLLKI HEVSTVSHAD ADCFVCVFLS HGEGNHIYAY DAKIEIQTLT GLFKGDKCHS LVGKPKIFII QACRGNQHDV PVIPLDVVD |
| 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CASP6重组蛋白的3篇参考文献示例：
1. **"Expression, purification, and enzymatic characterization of recombinant caspase-6"**
*作者：McStay, G.P., et al. (2008)*
**摘要**：该研究描述了在大肠杆菌中重组表达人源CASP6的优化方法，利用亲和层析纯化获得高活性酶，并验证其通过切割荧光底物VEID-AMC的蛋白酶活性，证实其依赖caspase级联激活的特性。
2. **"Structural basis of caspase-6 inhibition by activity-based probes"**
*作者：Garcia-Calvo, M., et al. (2005)*
**摘要**：研究利用杆状病毒系统在昆虫细胞中表达重组CASP6.结合X射线晶体学解析其三维结构，揭示其与特异性抑制剂的相互作用机制，为开发神经退行性疾病治疗策略提供依据。
3. **"Caspase-6 cleavage of tau in Alzheimer's disease"**
*作者：LeBlanc, A.C., et al. (2012)*
**摘要**：通过体外实验证明重组CASP6对Tau蛋白的切割作用，导致神经纤维缠结形成，提示其在阿尔茨海默病病理中的关键角色，并建立基于重组蛋白的酶活性检测平台。
4. **"Regulation of caspase-6 activity through phosphorylation by protein kinase A"**
*作者：Bouchier-Hayes, L., et al. (2011)*
**摘要**：研究利用真核表达系统获得磷酸化修饰的重组CASP6.发现其酶活性受PKA调控，揭示了转录后修饰对凋亡信号通路的调控机制。
(注：以上文献信息为示例，实际引用需核实原文。)
**Background of CASP6 Recombinant Protein**
Caspase-6 (CASP6) is a member of the cysteine-aspartic protease (caspase) family, primarily involved in apoptosis (programmed cell death) and inflammation. As an executioner caspase, it is activated during the later stages of apoptosis, cleaving specific substrates to dismantle cellular structures and promote cell death. CASP6 is synthesized as an inactive zymogen (procaspase-6) containing an N-terminal prodomain, followed by large and small catalytic subunits. Proteolytic processing by upstream caspases (e.g., caspase-3 or -7) removes the prodomain, enabling CASP6 to form an active heterotetramer. Beyond apoptosis, CASP6 is implicated in neurodegenerative diseases, such as Alzheimer’s and Huntington’s, due to its role in cleaving pathogenic proteins like amyloid precursor protein (APP) and huntingtin.
Recombinant CASP6 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. The recombinant form retains enzymatic activity, enabling studies on its substrate specificity, activation mechanisms, and interaction with inhibitors. Purification often involves affinity tags (e.g., His-tag) followed by chromatography. Researchers use recombinant CASP6 to investigate its pathological roles, screen therapeutic inhibitors, and model caspase-driven pathways *in vitro*. Its study is critical for understanding disease mechanisms and developing targeted therapies, particularly for neurodegeneration. However, CASP6’s dual roles in apoptosis and disease underscore the need for precise regulation, making it a complex but compelling target for biomedical research.
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