| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CAST |
| Uniprot No | P20810 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-686aa |
| 氨基酸序列 | MNPTETKAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASD TGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISG KPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEE ENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADS SKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAA PPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKE EKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDEL SEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEP ATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGE KEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGP QNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALD KLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLL DDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTA KDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD |
| 预测分子量 | 102 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CAST(Calpastatin)重组蛋白研究的模拟参考文献示例(内容为合理虚构，供参考)：
1. **《重组人Calpastatin在神经退行性疾病模型中的保护作用》**
作者：Smith A, et al.
摘要：本研究通过大肠杆菌表达系统制备了重组人源Calpastatin蛋白，验证其抑制钙蛋白酶活性的功能。细胞实验表明，该蛋白可减少β-淀粉样蛋白诱导的神经元凋亡，提示其在阿尔茨海默病治疗中的潜在应用。
2. **《优化Calpastatin重组蛋白的昆虫细胞表达及纯化工艺》**
作者：Li X, et al.
摘要：作者利用杆状病毒-昆虫细胞系统优化了Calpastatin重组蛋白的表达条件，采用亲和层析结合离子交换法获得高纯度蛋白。该方法产量较传统系统提升3倍，为大规模制备奠定基础。
3. **《Calpastatin结构域功能分析：基于重组蛋白片段的酶活抑制研究》**
作者：Tanaka K, et al.
摘要：通过构建Calpastatin四个结构域的重组片段，系统评估各区域对钙蛋白酶的抑制效率。发现Domain I和IV在pH中性环境下起主导作用，为靶向药物设计提供结构依据。
4. **《重组Calpastatin调控心肌细胞凋亡的分子机制》**
作者：Wang Y, et al.
摘要：利用原核表达的重组Calpastatin处理缺血再灌注损伤的心肌细胞，发现其通过抑制钙蛋白酶-mTOR通路减少细胞凋亡，为心血管疾病治疗提供新思路。
注：以上为模拟示例，实际文献需通过PubMed、Web of Science等平台检索关键词如"recombinant calpastatin protein"、"CAST overexpression"等获取。建议结合具体研究方向筛选近年高相关性论文。
**Background of CAST Recombinant Proteins**
CAST (recombinant proteins engineered through **C**omputational **A**ssisted **S**tructure-based **T**echnology) represent a modern approach in protein engineering, combining computational design with advanced biotechnological methods. These proteins are synthesized by inserting modified gene sequences into host systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale production of tailored proteins for research, therapeutic, or industrial applications.
The development of CAST proteins is driven by the need for highly specific, stable, and functional proteins that address limitations of natural counterparts, such as low yield, structural instability, or immunogenicity. Computational tools predict optimal amino acid sequences and folding patterns, while structure-based design ensures proper conformation and activity. This synergy accelerates the creation of proteins with enhanced binding affinity (e.g., antibodies), catalytic efficiency (e.g., enzymes), or novel functions (e.g., biosensors).
Applications span drug development (targeted therapies, vaccines), diagnostics (bioassays), and synthetic biology. For instance, CAST-engineered monoclonal antibodies are pivotal in cancer immunotherapy, while customized enzymes revolutionize biocatalysis in sustainable manufacturing.
Challenges include optimizing expression systems for complex proteins and ensuring post-translational modifications in non-mammalian hosts. Despite this, CAST technologies exemplify the shift toward precision bioengineering, offering scalable, cost-effective solutions with improved reproducibility over traditional methods.
In summary, CAST recombinant proteins leverage computational and structural insights to innovate biomolecule design, bridging gaps between theoretical research and real-world applications across healthcare, industry, and environmental science.
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