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Recombinant gltA protein

  • 中文名: 谷氨酸合酶(NADPH)大亚基(gltA)重组蛋白
  • 别    名: gltA;Glutamate synthase [NADPH] large chain
货号: PA2000-5026
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点gltA
Uniprot No P56062
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-426aa
氨基酸序列MSVTLVNNENNERYEFETIESTRGPKAVDFSKLFETTGFFSYDPGYSSTAGCQSKISYVNGKKGELYYRGHRIEDLVAKYKYVDVCKLLLTGELPKNQDESLEFELELRHRSFVHESLLNMFSAFPSNAHPMAKLSSGVSILSTLYSTHQNMHTEEDYQTMARRIVAKIPTLAAICYRNEVGAPIIYPDIARSYVENILFMLRGYPYSRLKHTTQGEVEITPLEVEAFDKILTLHADHSQNASSTTVRNVASTGVHPYAAISAGISALWGHLHGGANEKVLLQLEEIGDVKNVDKYIARVKDKNDNFKLMGFGHRVYKSYDPRAKILKGLKDELHQKGVKMDERLSEIAAKVEEIALKDEYFIERNLYPNVDFYSGTILRALKIPVRFFTPVFVIGRTVGWCAQLLEHVKSPQARITRPRQVYVGD
预测分子量55.9kDa
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gltA重组蛋白的示例参考文献(注:以下内容为示例性文献,供参考格式和内容):

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1. **文献名称**: "Expression and Functional Analysis of Recombinant gltA-Encoded Citrate Synthase from *Escherichia coli*"

**作者**: Smith J, Brown K, et al.

**摘要**: 本研究在大肠杆菌中成功克隆并表达了gltA基因编码的柠檬酸合酶。重组蛋白通过亲和层析纯化,并验证了其在三羧酸循环中的催化活性,为酶动力学研究提供了基础。

2. **文献名称**: "Crystal Structure of Recombinant gltA Protein from *Bacillus subtilis* and Its Role in Metabolic Regulation"

**作者**: Zhang Y, Wang L, et al.

**摘要**: 通过X射线晶体学解析了枯草芽孢杆菌来源的重组gltA蛋白的三维结构,揭示了其底物结合位点和催化机制,为开发新型代谢抑制剂提供了结构依据。

3. **文献名称**: "Heterologous Expression of gltA in *Saccharomyces cerevisiae* for Enhanced Citrate Production"

**作者**: Lee S, Kim H, et al.

**摘要**: 在酿酒酵母中异源表达gltA基因,重组蛋白显著提高了胞内柠檬酸合成效率,为微生物发酵生产有机酸提供了新策略。

4. **文献名称**: "Functional Characterization of a Thermophilic gltA Recombinant Protein from *Thermus thermophilus*"

**作者**: Müller R, Schmidt D, et al.

**摘要**: 从嗜热菌中克隆gltA基因并实现重组表达,纯化后的酶在高温下保持高活性,适用于工业生物催化过程。

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建议通过PubMed、Google Scholar等平台,以关键词“gltA recombinant protein expression”或“citrate synthase gltA”检索最新文献,以获取真实研究数据。

背景信息

**Background of gltA Recombinant Protein**

The *gltA* gene encodes citrate synthase (CS), a key enzyme in the tricarboxylic acid (TCA) cycle, catalyzing the condensation of acetyl-CoA and oxaloacetate to form citrate. This reaction represents the first committed step of the TCA cycle, linking carbohydrate, lipid, and amino acid metabolism. Due to its central role in cellular energy production and biosynthesis, citrate synthase is evolutionarily conserved across prokaryotes and eukaryotes, making it a critical target for metabolic studies.

In pathogenic organisms, *gltA* has garnered attention as a potential therapeutic target. For instance, in *Mycobacterium tuberculosis*, *gltA* is essential for survival, and its inhibition disrupts bacterial metabolism. Similarly, in *Borrelia burgdorferi* (the causative agent of Lyme disease), *gltA* is vital for energy metabolism, highlighting its broad relevance in microbial pathogenesis.

Recombinant gltA protein is typically produced via heterologous expression in systems like *Escherichia coli* or yeast, enabling large-scale purification for functional and structural analyses. The recombinant protein retains enzymatic activity, allowing researchers to study its kinetics, substrate specificity, and interactions with potential inhibitors. Advanced techniques such as X-ray crystallography and cryo-EM have resolved its 3D structure, revealing insights into catalytic mechanisms and allosteric regulation.

Beyond basic research, gltA recombinant protein is utilized in diagnostic assays (e.g., detecting *Coxiella burnetii* infections) and vaccine development. Its immunogenicity in pathogens like *Brucella spp.* has spurred interest in subunit vaccines. Additionally, gltA-based studies contribute to synthetic biology, where engineered TCA pathways optimize microbial production of biofuels or bioproducts.

Overall, gltA recombinant protein serves as a versatile tool bridging fundamental biochemistry, antimicrobial discovery, and biotechnological applications, underscoring its multifaceted importance in both academic and translational research.

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