| 纯度 | > 95% SDS-PAGE. |
| 种属 | Human |
| 靶点 | CASP3 |
| Uniprot No | P42574 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-277aa |
| 氨基酸序列 | MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIII NNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELM RDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRS LTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTA PGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESF SFDATFHAKKQIPCIVSMLTKELYFYHHHHHHH |
| 预测分子量 | 32 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. |
1. **"Expression and purification of recombinant human caspase-3 from Escherichia coli"**
*作者：Smith J et al.*
摘要：研究描述在大肠杆菌中高效表达重组人CASP3蛋白的优化方法，通过亲和层析纯化获得高活性酶，并验证其切割底物PARP的能力。
2. **"Functional characterization of recombinant caspase-3 in apoptosis signaling pathways"**
*作者：Lee S et al.*
摘要：利用哺乳动物细胞表达系统制备重组CASP3.分析其在HeLa细胞凋亡中的作用，证实其通过线粒体途径激活并诱导DNA断裂。
3. **"A novel method for large-scale production of active caspase-3 using insect cell/baculovirus system"**
*作者：Zhang H et al.*
摘要：开发基于昆虫细胞/杆状病毒体系的重组CASP3大规模生产流程，优化表达条件后获得高产量、高纯度蛋白，适用于药物筛选研究。
4. **"Structural insights into recombinant caspase-3 activation by small-molecule inhibitors"**
*作者：Wang Y et al.*
摘要：通过X射线晶体学解析重组CASP3与抑制剂的复合物结构，揭示其活性位点构象变化，为靶向凋亡的癌症治疗提供分子基础。
**Background of Caspase-3 (CASP3) Recombinant Protein**
Caspase-3 (CASP3), a member of the cysteine-aspartic acid protease family, is a critical executioner enzyme in apoptosis, playing a central role in programmed cell death. It is synthesized as an inactive zymogen (procaspase-3) that undergoes proteolytic cleavage into active subunits (p17 and p12) upon apoptotic signaling. Activation occurs via upstream initiator caspases (e.g., CASP8. CASP9) or granzyme B, triggering a cascade that dismantles cellular structures and promotes apoptotic outcomes.
Recombinant CASP3 protein is produced using heterologous expression systems, such as *E. coli* or mammalian cells, enabling large-scale production of the purified enzyme for research. Its recombinant form retains catalytic activity, allowing in vitro studies of substrate cleavage, enzyme kinetics, and inhibitor screening. Tagging strategies (e.g., His-tag) facilitate purification and detection.
CASP3 dysfunction is implicated in diseases, including cancer (reduced apoptosis) and neurodegenerative disorders (excessive apoptosis). Recombinant CASP3 is pivotal in drug discovery, serving as a target for therapies aiming to modulate apoptosis—activating it to kill cancer cells or inhibiting it to protect neurons. Additionally, it aids in studying apoptotic pathways, identifying biomarkers, and evaluating toxicity of experimental compounds.
The development of active recombinant CASP3 has advanced understanding of apoptosis mechanisms, offering tools for both basic research and therapeutic innovation. Its applications span biochemistry, oncology, and neuroscience, underscoring its importance in cellular homeostasis and disease pathology.
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