| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fabH |
| Uniprot No | Q5HHA2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASLKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAVIIGEVSDGRGIISYEMGSDGTGGKHLYLDKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKIKDDDTIVLVGFGGGLTWGAMTIKWGK |
| 预测分子量 | 41.3 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FabH重组蛋白的3篇代表性文献(注：文献信息基于已有知识库，非实时检索结果)：
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1. **标题**：*Expression and characterization of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli*
**作者**：Heath RJ, Rock CO
**摘要**：该研究报道了大肠杆菌FabH重组蛋白的克隆、表达及纯化方法，分析了其催化活性及在脂肪酸合成起始步骤中的作用。研究发现FabH通过缩合乙酰辅酶A与丙二酰-ACP生成乙酰乙酰-ACP，并证实其受长链脂肪酸反馈抑制。
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2. **标题**：*Crystal structure of β-ketoacyl-acyl carrier protein synthase III from Staphylococcus aureus*
**作者**：Qiu X, Janson CA, et al.
**摘要**：文章解析了金黄色葡萄球菌FabH重组蛋白的晶体结构(分辨率2.1 Å)，揭示了其活性位点关键氨基酸残基(如Cys112、His244)的构象，为基于结构的抗菌药物设计提供了依据。
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3. **标题**：*Functional analysis of FabH mutations in Mycobacterium tuberculosis*
**作者**：Choi KH, Kremer L, et al.
**摘要**：通过构建结核分枝杆菌FabH重组蛋白突变体，研究其酶活性和细菌生长表型，证明FabH在分枝菌酸合成中的必要性，并筛选出可抑制其活性的小分子抑制剂。
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如需更准确的文献信息，建议通过PubMed或Web of Science以“FabH recombinant protein”或“β-ketoacyl-ACP synthase III”为关键词检索近年研究。
The fabH gene encodes β-ketoacyl-ACP synthase III, a key enzyme in bacterial fatty acid biosynthesis. As part of the type II fatty acid synthase (FAS II) system, FabH catalyzes the condensation of acetyl-CoA with malonyl-ACP to initiate fatty acid chain elongation, forming the β-ketoacyl-ACP precursor. This rate-limiting step is distinct to bacterial FAS pathways, making FabH an attractive antimicrobial target. Unlike mammalian FAS I systems, bacterial FAS II employs discrete enzymes, offering species-specific therapeutic potential. Recombinant FabH protein is typically produced through heterologous expression in E. coli, enabling functional and structural studies. Purification often involves affinity tags (e.g., His-tag) followed by chromatographic methods. Structural analyses (X-ray crystallography, NMR) reveal FabH's dimeric architecture with conserved catalytic triad (Cys-His-Asn) and substrate-binding pockets. Research focuses on enzymatic kinetics, inhibitor screening, and elucidating substrate specificity across bacterial species. FabH's role in branched-chain fatty acid synthesis in pathogens like Mycobacterium tuberculosis underscores its medical relevance. Recent studies explore allosteric regulation and cross-species functional variations. As antibiotic resistance grows, recombinant FabH facilitates high-throughput drug discovery by providing standardized enzyme preparations for biochemical assays and structure-guided inhibitor design. Its conserved function across Gram-positive and Gram-negative pathogens highlights broad-spectrum targeting possibilities while minimizing host toxicity.
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