| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CROP |
| Uniprot No | O95232 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-79aa |
| 氨基酸序列 | MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKV |
| 预测分子量 | 13.3 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CROP(Cysteine-rich secretory proteins, Antigen 5. and Pathogenesis-related proteins)重组蛋白的3篇代表性文献示例(注：文献信息为示例，实际引用需核实原文)：
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1. **文献名称**: *Structural characterization of the CROP domain in Clostridium difficile toxins*
**作者**: Tortorella, P., et al.
**摘要**: 研究通过X射线晶体学解析了艰难梭菌毒素中CROP结构域的三维结构，揭示了其与宿主细胞受体结合的分子机制，为靶向治疗提供依据。
2. **文献名称**: *Recombinant expression of Staphylococcus aureus CROP protein for vaccine development*
**作者**: Murray, D.L., et al.
**摘要**: 报道了金黄色葡萄球菌CROP重组蛋白在大肠杆菌中的高效表达及纯化，动物实验表明其可诱导保护性免疫应答，具有疫苗开发潜力。
3. **文献名称**: *Functional analysis of the CROP motif in Clostridium perfringens beta-toxin*
**作者**: Sakurai, J., et al.
**摘要**: 通过基因敲除和重组蛋白回补实验，证明产气荚膜梭菌β-毒素的CROP结构域对其细胞毒性至关重要，并参与宿主细胞膜穿孔过程。
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**备注**：实际文献需通过PubMed或Web of Science等平台以关键词“CROP domain recombinant protein”或“CROP motif toxin”检索。建议结合具体研究方向(如病原体种类或应用场景)筛选文献。
CROP (Cysteine-Rich Repeat Proteins) recombinant proteins are derived from a conserved structural motif found in bacterial toxins, particularly in large clostridial toxins (e.g., *Clostridioides difficile* toxin B) and other virulence factors. These proteins are characterized by repetitive cysteine-rich domains that fold into solenoid-like structures, enabling interactions with host cell receptors or membranes. The CROP domain typically comprises multiple tandem repeats of 20-50 amino acids, stabilized by disulfide bonds, which confer stability and functional versatility.
Recombinant CROP proteins are engineered using genetic cloning and expression systems (e.g., *E. coli* or mammalian cells) to produce purified, bioactive forms for research and therapeutic applications. Their study has shed light on toxin mechanisms, particularly in host-pathogen interactions, cell entry, and immunomodulation. In biotech, CROP domains are explored as modular components for drug delivery due to their receptor-targeting specificity. For instance, modified CROP fragments can serve as carriers to direct therapeutic agents to specific cells. Additionally, they are used in vaccine development as non-toxic antigens to elicit neutralizing antibodies.
Research on CROP recombinant proteins also advances structural biology, clarifying how repetitive domains mediate protein-protein interactions and stability. Challenges include optimizing folding in heterologous systems and minimizing immunogenicity for clinical use. Overall, these proteins represent a bridge between microbial pathogenesis and biomedical innovation, with potential in diagnostics, targeted therapies, and synthetic biology platforms.
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