| 纯度 | >90%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | IdhA |
| Uniprot No | P52643 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-329aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV |
| 预测分子量 | 39 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IdhA/IDH1重组蛋白的3篇参考文献，简要整理如下：
1. **标题**：Expression and characterization of recombinant human IDH1 mutants
**作者**：Dang L, et al.
**摘要**：研究团队在大肠杆菌中表达了携带R132H/R132C突变的IDH1重组蛋白，证实突变体催化α-KG转化为2-HG的能力，为胶质瘤代谢机制提供依据。
2. **标题**：Structural basis for the mechanism of substrate inhibition in human IDH1
**作者**：Xu X, et al.
**摘要**：通过表达并纯化人源IDH1重组蛋白，结合X射线晶体学解析其结构，揭示了底物异柠檬酸在高浓度下抑制酶活性的分子机制。
3. **标题**：Cloning and functional analysis of Escherichia coli IdhA gene encoding NADP+-dependent isocitrate dehydrogenase
**作者**：Dean J, et al.
**摘要**：克隆大肠杆菌idhA基因并在原核系统中重组表达，验证其编码的NADP+依赖型异柠檬酸脱氢酶活性，探究其在TCA循环中的功能。
备注：若需扩展，可补充IDH2相关研究或特定应用(如癌症诊断试剂开发)的文献。
IdhA, encoding the enzyme isocitrate dehydrogenase (IDH), plays a central role in the tricarboxylic acid (TCA) cycle, catalyzing the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG) while reducing NAD⁺ to NADH. This reaction is critical for cellular energy production, redox balance, and the generation of biosynthetic precursors in microorganisms, including Escherichia coli. In metabolic engineering and industrial biotechnology, IdhA has garnered significant attention due to its regulatory influence on carbon flux distribution between the TCA cycle and alternative pathways, such as the glyoxylate shunt or anaerobic fermentation.
Recombinant IdhA protein production typically involves heterologous expression in E. coli using plasmid-based systems. The enzyme is often cloned with affinity tags (e.g., His-tag) to facilitate purification via immobilized metal affinity chromatography. Structural and functional studies of recombinant IdhA have provided insights into its catalytic mechanism, cofactor specificity (NAD⁺ vs. NADP⁺), and allosteric regulation, which varies across species. For instance, bacterial IDHs are usually NAD⁺-dependent, while eukaryotic isoforms frequently utilize NADP⁺.
In biotechnological applications, IdhA manipulation serves dual purposes. Its deletion or downregulation redirects carbon flux toward succinate or acetate production in microbial cell factories, enhancing yields of platform chemicals. Conversely, overexpression of recombinant IdhA can optimize α-KG synthesis, a valuable compound in food additives, pharmaceuticals, and as a precursor for glutamate production. Recent advances also explore engineered IDH variants with altered cofactor preferences or improved thermostability for industrial biocatalysis. Furthermore, IdhA-based metabolic engineering supports sustainable bioproduction of biofuels and bioplastics by balancing NADH/ATP levels and minimizing byproduct formation. These applications underscore IdhA's versatility as both a metabolic engineering target and a tool enzyme in synthetic biology.
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