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Recombinant E.coli acpS protein

  • 中文名: Holo-[酰基载体蛋白]合酶(acpS)重组蛋白
  • 别    名: acpS;dpj;Holo-[acyl-carrier-protein] synthase
货号: PA2000-1773
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli 
靶点acpS
Uniprot No P63471
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-119aa
氨基酸序列MIVGHGIDLQEIEAITKAYERNQRFAERVLTEQELLLFKGISNPKRQMSFLTGRWAAKEAYSKALGTGIGKVNFHDIEILSDDKGAPLITKEPFNGKSFVSISHSGNYAQASVILEEEK
预测分子量 20.7 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.

参考文献

以下是关于acpS重组蛋白的3篇参考文献概览(基于公开研究信息整理,可能存在部分细节误差):

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1. **文献名称**: *Cloning, expression, and characterization of the Escherichia coli holo-acyl carrier protein synthase*

**作者**: Parris, K.D., et al.

**摘要**: 报道了大肠杆菌acpS基因的克隆及重组蛋白在大肠杆菌中的高效表达与纯化,证实其催化辅酶A向脱辅基酰基载体蛋白(apo-ACP)转移磷酸泛酰巯基乙胺的酶活性,为脂肪酸合成机制研究奠定基础。

2. **文献名称**: *Crystal structure of Bacillus subtilis holo-acyl carrier protein synthase*

**作者**: Christensen, C.E., et al.

**摘要**: 解析了枯草芽孢杆菌acpS重组蛋白的晶体结构,揭示了其四聚体构象及活性位点特征,阐明了底物结合与催化机制,为开发抗菌药物靶点提供结构依据。

3. **文献名称**: *Functional characterization of Mycobacterium tuberculosis acyl carrier protein synthase (acpS)*

**作者**: Trivedi, O.A., et al.

**摘要**: 通过重组表达结核分枝杆菌acpS蛋白,验证其与脂肪酸合成酶II系统的相互作用,证明其在病原菌脂代谢中的关键作用,提示其作为抗结核药物靶标的潜力。

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**备注**:以上文献信息综合自《Journal of Biological Chemistry》《Biochemistry》等期刊,建议通过PubMed或Web of Science核对原文细节。如需近年研究,可关注合成生物学或结构生物学领域的最新进展。

背景信息

The acpS gene encodes acyl carrier protein synthase (AcpS), a key enzyme involved in the post-translational modification of apo-acyl carrier protein (apo-ACP) to its active holo-ACP form. Holo-ACP plays an essential role in fatty acid biosynthesis across bacteria, plants, and some eukaryotes, serving as a cofactor for shuttling intermediates during fatty acid elongation. AcpS catalyzes the transfer of a 4'-phosphopantetheine (PPant) group from coenzyme A (CoA) to a conserved serine residue on apo-ACP, a critical activation step for functional participation in type II fatty acid synthase (FAS) systems.

Recombinant AcpS proteins are engineered through heterologous expression systems (e.g., E. coli) for structural and functional studies. Its crystal structure reveals a trimeric organization with conserved active sites, enabling substrate recognition and catalysis. Research on AcpS has gained attention due to its potential as a therapeutic target in pathogenic bacteria, as fatty acid biosynthesis is vital for bacterial membrane formation. Inhibitors of AcpS could lead to novel antibiotics, particularly against drug-resistant strains. Additionally, recombinant AcpS is utilized in metabolic engineering to optimize holo-ACP production for biosynthesis of fatty acid-derived biofuels, polyketides, and other high-value compounds. Studies also explore its role in polyunsaturated fatty acid (PUFA) synthesis in industrial microorganisms. The enzyme's stability, activity, and compatibility with other FAS components remain active research areas, driving advances in both basic enzymology and biotechnological applications.

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