| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ACP |
| Uniprot No | P0A6A8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-78aa |
| 氨基酸序列 | MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDYINGHQA |
| 预测分子量 | 8,6 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ACP重组蛋白的3篇参考文献示例(文献信息为模拟示例，非真实文献)：
1. **文献名称**：*High-yield expression and purification of recombinant Acyl Carrier Protein (ACP) in E. coli*
**作者**：Smith, J. et al.
**摘要**：研究报道了通过优化大肠杆菌表达系统实现ACP的高效重组表达，采用亲和层析技术纯化获得高纯度ACP，并验证其在体外脂肪酸合成中的功能活性。
2. **文献名称**：*Structural characterization of recombinant ACP from Streptomyces species and its role in polyketide biosynthesis*
**作者**：Li, X. & Wang, Y.
**摘要**：通过X射线晶体学解析了链霉菌来源重组ACP的三维结构，揭示了其与聚酮合酶相互作用的特定结构域，为工程化改造聚酮合成途径提供依据。
3. **文献名称**：*Functional analysis of plant-derived ACP recombinant protein in lipid metabolism*
**作者**：Chen, R. et al.
**摘要**：将拟南芥ACP基因克隆至酵母表达系统，证明重组ACP可恢复脂肪酸合成缺陷型菌株的生长，阐明其在植物脂质代谢中的保守功能及潜在应用价值。
注：以上文献为示例，实际引用时请核实真实数据库(如PubMed、Web of Science)中的最新文献。
ACP (Acyl Carrier Protein) recombinant protein is a key biomolecule derived from genetic engineering techniques, widely utilized in studies of fatty acid biosynthesis and metabolic engineering. Originally identified in the 1960s as a critical component of bacterial fatty acid synthesis, ACP serves as a universal carrier of acyl intermediates during chain elongation. Its small, acidic structure (approx. 8-10 kDa) contains a conserved serine residue that binds phosphopantetheine groups, enabling thioester bonding with fatty acid substrates.
The development of recombinant ACP emerged alongside advances in molecular cloning. By inserting the *acpP* gene (or homologs from various organisms) into expression vectors, researchers can produce high-purity ACP in systems like *E. coli*. This recombinant approach overcomes limitations of native protein extraction, allowing scalable production and site-specific modifications. Histidine tags or fluorescent markers are often incorporated for purification and tracking.
Recombinant ACP has become indispensable in synthetic biology and enzyme mechanism studies. It facilitates in vitro reconstitution of fatty acid synthases, aids in probing acyltransferase specificity, and serves as a scaffold for engineering novel biosynthetic pathways. Recent applications extend to producing biofuels, polyketides, and hybrid natural products. Modified ACP variants are also explored as biosensors for metabolic flux analysis.
Commercial availability since the 2000s has accelerated its adoption in both academic and industrial settings. Ongoing research focuses on optimizing thermostability, improving carrier efficiency in non-native systems, and developing ACP-linked tools for metabolic engineering in microbes and plants.
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