| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CASP7 |
| Uniprot No | P55210 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-303aa |
| 氨基酸序列 | MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKT TRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKC FRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVI YGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSG PINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILE EHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELY FSQHHHHHH |
| 预测分子量 | 35 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CASP7重组蛋白的3篇代表性文献的简要概括：
1. **文献名称**：*Expression, purification, and characterization of recombinant caspase-7*
**作者**：Smith DM, et al.
**摘要**：该研究描述了一种在大肠杆菌中高效表达人源CASP7重组蛋白的方法，并通过亲和层析和离子交换层析纯化获得高活性蛋白，验证了其通过底物切割实验的酶活性。
2. **文献名称**：*Crystal structure of procaspase-7 in complex with a tetrapeptide inhibitor*
**作者**：Chai J, et al.
**摘要**：通过X射线晶体学解析了重组CASP7酶原与抑制剂的复合物结构，揭示了其激活过程中构象变化的关键机制，为设计靶向CASP7的药物提供了结构基础。
3. **文献名称**：*Role of caspase-7 in apoptosis induced by DNA-damaging agents*
**作者**：Lakhani SA, et al.
**摘要**：利用重组CASP7蛋白及基因敲除细胞模型，证明CASP7在DNA损伤诱导的凋亡通路中起关键作用，并发现其与CASP3的功能协同性。
4. **文献名称**：*Recombinant caspase-7 production in mammalian cells and its application in screening small molecule modulators*
**作者**：Wang Y, et al.
**摘要**：开发了一种在哺乳动物细胞中表达重组CASP7的方法，并基于此建立高通量筛选平台，成功鉴定出多个调控其活性的小分子化合物。
(注：上述文献为示例性质，实际引用时请核实具体文献信息。)
Caspase-7 (CASP7), a member of the cysteine-aspartic protease (caspase) family, is a key executioner enzyme in apoptosis. It exists as an inactive procaspase-7 zymogen that undergoes proteolytic activation during apoptotic signaling, typically by upstream initiator caspases (e.g., caspase-9) or other proteases. Once activated, CASP7 cleaves specific cellular substrates, including structural proteins and DNA repair enzymes, leading to controlled cell dismantling. Its role extends beyond apoptosis, with implications in inflammation, differentiation, and immune response regulation.
Recombinant CASP7 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to ensure high purity and activity. The recombinant form retains the native enzyme's functional domains, including the catalytic cysteine residue critical for protease activity. Researchers utilize recombinant CASP7 to study apoptotic mechanisms, screen caspase inhibitors, or model diseases linked to dysregulated apoptosis, such as cancer or neurodegenerative disorders. Structural studies of recombinant CASP7 have revealed insights into its substrate-binding pockets and activation mechanisms, aiding drug design.
Notably, CASP7’s substrate specificity overlaps with caspase-3 but displays unique regulatory features, making it a distinct therapeutic target. Dysregulation of CASP7 is associated with chemotherapy resistance and autoimmune diseases. Recombinant protein tools enable functional assays (e.g., fluorogenic substrate cleavage) and mechanistic exploration of caspase cascades. Its production under controlled conditions ensures batch-to-batch consistency, critical for both basic research and preclinical applications targeting apoptotic pathways.
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