| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | acpH |
| Uniprot No | P21515 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-193aa |
| 氨基酸序列 | MNFLAHLHLAHLAESSLSGNLLADFVRGNPEESFPPDVVAGIHMHRRIDVLTDNLPEVREAREWFRSETRRVAPITLDVMWDHFLSRHWSQLSPDFPLQEFVCYAREQVMTILPDSPPRFINLNNYLWSEQWLVRYRDMDFIQNVLNGMASRRPRLDALRDSWYDLDAHYDALETRFWQFYPRMMAQASRKAL |
| 预测分子量 | 30.4 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3篇与acpH重组蛋白相关的模拟参考文献(内容基于常见研究方向构建，实际文献需通过数据库核实)：
1. **文献名称**: "Expression and purification of recombinant acpH protein from Escherichia coli: enzymatic characterization and functional analysis"
**作者**: Zhang L, et al.
**摘要**: 研究报道了acpH基因在大肠杆菌中的重组表达与镍柱纯化流程，证实其编码的酸性磷酸酶活性依赖镁离子，最适pH为6.5.并揭示其在细菌乙酰辅酶A代谢中的调控作用。
2. **文献名称**: "Crystal structure of acpH reveals a novel metallophosphatase fold involved in bacterial acyl-carrier protein hydrolysis"
**作者**: Thompson JR, White SW.
**摘要**: 通过X射线晶体学解析acpH蛋白的三维结构，发现其具有独特的金属磷酸酶结构域，阐明了其通过水解酰基载体蛋白(ACP)硫酯键参与脂肪酸合成的分子机制。
3. **文献名称**: "Functional interplay between acpH and lipid biosynthesis in Pseudomonas aeruginosa biofilm formation"
**作者**: Gupta R, et al.
**摘要**: 研究证明铜绿假单胞菌中acpH通过调节脂质前体供应影响生物被膜形成，敲除acpH导致细菌胞外多糖合成减少，为针对细菌耐药性的靶点开发提供依据。
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**注**：以上为模拟文献，实际研究中建议通过PubMed、Web of Science等平台以“acpH recombinant protein”“acpH phosphatase”等关键词检索，重点关注《Journal of Bacteriology》《Biochemistry》等微生物与生化领域期刊。
acpH (acyl carrier protein phosphodiesterase) is a bacterial enzyme involved in fatty acid metabolism, primarily studied in model organisms like *Escherichia coli*. It catalyzes the hydrolysis of the phosphodiester bond in acyl carrier protein (ACP)-bound intermediates, releasing inorganic phosphate and modulating the availability of ACP for fatty acid biosynthesis. ACP is a critical cofactor in fatty acid synthesis, shuttling growing acyl chains between enzymatic complexes. By regulating ACP recycling, acpH influences metabolic flux, ensuring balanced lipid biosynthesis and cellular membrane homeostasis.
Recombinant acpH protein is produced through genetic engineering, typically by cloning the *acpH* gene into expression vectors (e.g., plasmid systems) and overexpressing it in host cells like *E. coli*. Purification involves affinity chromatography, leveraging tags such as His-tags for efficient isolation. This recombinant tool enables detailed biochemical studies, including enzymatic activity assays, structural analysis (e.g., X-ray crystallography), and interaction mapping with ACP or inhibitors.
Research on acpH has implications for understanding bacterial lipid metabolism and developing antimicrobial agents. Since fatty acid synthesis pathways are essential for bacterial survival but distinct from eukaryotic systems, acpH represents a potential drug target. Inhibitors could disrupt membrane biosynthesis in pathogens without affecting human cells. Additionally, acpH studies contribute to synthetic biology applications, such as engineering microbial strains for optimized lipid production in biofuels or biomanufacturing. Its role in metabolic regulation also intersects with studies on bacterial persistence, antibiotic tolerance, and stress responses, making it a multifaceted subject in both basic and applied microbiology.
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