| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ACHAP |
| Uniprot No | O60888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-179aa |
| 氨基酸序列 | RLLLLPRV LLTMASGSPP TQPSPASDSG SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI PQITSIYEWK GKIEEDSEVL MMIKTQSSLV PALTDFVRSV HPYEVAEVIA LPVEQGNFPY LQWVRQVTES VSDSITVLP |
| 预测分子量 | 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ACHAP重组蛋白的假设性参考文献示例(基于常见重组蛋白研究方向模拟，供参考)：
1. **文献名称**：Expression and Purification of ACHAP Recombinant Protein in E. coli
**作者**：Zhang L, et al.
**摘要**：本研究成功构建了ACHAP基因的原核表达载体，通过大肠杆菌系统实现高效表达。优化后的纯化工艺可获得高纯度蛋白，为后续功能研究奠定基础。
2. **文献名称**：ACHAP Recombinant Protein Enhances Antiviral Immunity in Mouse Models
**作者**：Wang Y, et al.
**摘要**：研究发现ACHAP重组蛋白能显著激活巨噬细胞TLR4通路，提升干扰素分泌，在流感病毒小鼠模型中降低肺组织病毒载量，提示其免疫调节潜力。
3. **文献名称**：Structural Characterization of ACHAP Protein by Cryo-EM
**作者**：Chen X, et al.
**摘要**：通过冷冻电镜解析ACHAP重组蛋白的3.2Å三维结构，揭示其独特的α-螺旋结构域与配体结合位点，为靶向药物设计提供结构基础。
4. **文献名称**：Industrial-scale Production of ACHAP Using Mammalian Cell Culture
**作者**：Tanaka K, et al.
**摘要**：开发基于CHO细胞的悬浮培养工艺，实现ACHAP蛋白的克级产量，糖基化修饰分析显示与天然蛋白高度一致，满足临床前研究需求。
注：以上文献为模拟示例，实际研究中请通过学术数据库检索具体文献。建议结合研究领域补充关键词(如"ACHAP vaccine"或"ACHAP cancer")以提高检索准确性。
ACHAP recombinant protein is a hybrid biomolecule engineered by combining functional domains from distinct protein families to achieve synergistic biological activities. The acronym ACHAP typically refers to a fusion construct incorporating an anchoring module (e.g., albumin-binding domains or cell-penetrating peptides) and a CHAP (Cysteine Histidine-dependent Amidohydrolase/Peptidase) domain derived from bacterial endolysins or enzymatically active bacteriophage proteins. This design aims to enhance target specificity, stability, and therapeutic efficacy compared to native enzymes.
The CHAP domain, conserved across diverse microbial systems, exhibits hydrolytic activity against bacterial cell wall peptidoglycans, making it particularly valuable in antimicrobial applications. When fused with an anchoring component, ACHAP proteins gain improved tissue retention and cellular internalization capabilities. For instance, albumin-binding domains extend serum half-life by leveraging natural albumin recycling pathways, while cell-penetrating sequences facilitate intracellular delivery against pathogenic bacteria hiding in host cells.
Developed primarily for biomedical applications, ACHAP recombinant proteins have shown promise in addressing antibiotic-resistant infections. Their modular architecture allows customization against specific pathogens like Staphylococcus aureus or Streptococcus pneumoniae by modifying the catalytic domain’s substrate specificity. Beyond antimicrobial uses, engineered ACHAP variants are explored in biotechnology for biofilm disruption, targeted drug delivery, and protein-based diagnostic tools. Current research focuses on optimizing pharmacokinetic profiles and minimizing immunogenicity while maintaining enzymatic potency under physiological conditions. This innovative protein engineering approach bridges bacteriolytic activity with enhanced biodistribution, representing a growing trend in precision antimicrobial therapeutics.
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