| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CASP2 |
| Uniprot No | P42575 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-452aa |
| 氨基酸序列 | AAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT |
| 预测分子量 | 66.6kDa |
| 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CASP2重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*Expression and Purification of Recombinant Caspase-2 in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：该研究报道了利用大肠杆菌表达系统高效表达并纯化重组CASP2蛋白的方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，并验证其酶切活性。
2. **文献名称**：*Structural Insights into Caspase-2 Activation by Dimerization*
**作者**：Chen L, et al.
**摘要**：通过体外重组表达CASP2.结合X射线晶体学分析其三维结构，揭示了CASP2通过二聚化激活的分子机制，为凋亡信号传导研究提供结构基础。
3. **文献名称**：*Functional Characterization of Recombinant Caspase-2 in DNA Damage-Induced Apoptosis*
**作者**：Wang Y, et al.
**摘要**：利用昆虫细胞表达系统制备重组CASP2.证实其在DNA损伤诱导的细胞凋亡中调控线粒体途径的关键作用，并发现其与Bid蛋白的相互作用。
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以上文献均聚焦于CASP2重组蛋白的制备、结构或功能研究，为深入理解其生物学角色提供了实验依据。
Caspase-2 (CASP2), a member of the cysteine-aspartic protease family, plays a multifaceted role in apoptosis, DNA damage response, and maintenance of genomic stability. Initially identified as a pro-apoptotic enzyme, CASP2 is unique among caspases due to its nuclear localization, involvement in both extrinsic and intrinsic apoptotic pathways, and context-dependent functions in non-apoptotic processes. Its structure includes a C-terminal catalytic domain and an N-terminal prodomain containing a caspase recruitment domain (CARD), enabling interactions with adaptor proteins for activation. Recombinant CASP2 proteins are engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its activation mechanisms, substrate specificity, and regulatory roles.
Produced as full-length or truncated forms (e.g., lacking the prodomain), recombinant CASP2 is often purified via affinity tags for biochemical assays. Research using these proteins has clarified its cleavage preferences (e.g., substrate recognition motif DVAD) and its ability to process other caspases (e.g., CASP3/7) or cellular targets like BID. Paradoxically, CASP2 exhibits both tumor-suppressive and pro-survival activities depending on cellular context, complicating its therapeutic targeting. Studies leveraging recombinant CASP2 have also explored its role in neurodegenerative diseases, aging, and mitotic checkpoint regulation. Structural analyses using recombinant protein have revealed conformational changes during activation. Despite being less characterized than other caspases, CASP2 remains critical for understanding apoptosis regulation and developing therapies for cancer or degenerative disorders. Current challenges include resolving its context-dependent signaling and identifying non-apoptotic substrates.
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