| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gldA |
| Uniprot No | P32816 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-370aa |
| 氨基酸序列 | MAAERVFISP AKYVQGKNVI TKIANYLEGI GNKTVVIADE IVWKIAGHTI VNELKKGNIA AEEVVFSGEA SRNEVERIAN IARKAEAAIV IGVGGGKTLD TAKAVADELD AYIVIVPTAA STDAPTSALS VIYSDDGVFE SYRFYKKNPD LVLVDTKIIA NAPPRLLASG IADALATWVE ARSVIKSGGK TMAGGIPTIA AEAIAEKCEQ TLFKYGKLAY ESVKAKVVTP ALEAVVEANT LLSGLGFESG GLAAAHAIHN GFTALEGEIH HLTHGEKVAF GTLVQLALEE HSQQEIERYI ELYLSLDLPV TLEDIKLKDA SREDILKVAK AATAEGETIH NAFNVTADDV ADAIFAADQY AKAYKEKHRK |
| 预测分子量 | 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 **gldA重组蛋白** 的3篇参考文献及简要摘要：
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1. **文献名称**：*Cloning, expression, and characterization of glycerol dehydrogenase from *Bacillus subtilis* in *Escherichia coli***
**作者**：Wang et al.
**摘要**：该研究通过将枯草芽孢杆菌的gldA基因克隆至大肠杆菌中实现重组表达，纯化后的甘油脱氢酶(GDH)在催化甘油生成二羟丙酮(DHA)时表现出高活性，并验证了其在生物催化中的潜在应用价值。
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2. **文献名称**：*Enzymatic characterization of a recombinant glycerol dehydrogenase from *Streptomyces coelicolor* for chiral diol synthesis*
**作者**：Li et al.
**摘要**：研究报道了天蓝色链霉菌gldA基因的重组表达及酶学性质分析，证明该重组酶在非水相体系中高效催化手性二醇合成，为手性药物中间体制备提供了新策略。
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3. **文献名称**：*Optimization of recombinant glycerol dehydrogenase production in *Pichia pastoris* for industrial biocatalysis*
**作者**：Zhang et al.
**摘要**：通过毕赤酵母系统优化gldA重组蛋白的表达条件，显著提高酶产量和热稳定性，为工业化生产DHA及生物燃料电池应用奠定基础。
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The gldA gene, encoding glycerol dehydrogenase (EC 1.1.1.6), is a key enzyme in microbial glycerol metabolism. Originally identified in bacteria like Bacillus subtilis, it catalyzes the oxidation of glycerol to dihydroxyacetone (DHA) using NAD+ as a cofactor. This reaction plays critical roles in carbon utilization, osmoprotection, and redox balance. The enzyme's ability to interconvert polyols and ketoses has attracted biotechnological interest, particularly for DHA production—a valuable chemical in cosmetics, pharmaceuticals, and food industries.
Recombinant gldA protein production typically involves cloning the gene into expression vectors (e.g., pET or pGEX systems) followed by heterologous expression in hosts like E. coli. Optimization of induction conditions (temperature, IPTG concentration) and codon adaptation are often required to achieve soluble, active enzyme. Purification methods commonly exploit affinity tags (His-tag, GST-tag) with subsequent characterization of kinetic parameters and substrate specificity.
Interest in gldA extends beyond its native metabolic context. Engineered variants are explored for improved thermostability and expanded substrate range, enabling applications in biosensors for glycerol quantification and cascade reactions for chiral alcohol synthesis. In synthetic biology, gldA serves as a metabolic module for converting low-value glycerol byproducts from biodiesel production into higher-value compounds. Recent studies also investigate its potential in bioelectrochemical systems and NAD+ regeneration platforms. Despite progress, challenges remain in balancing enzyme activity with cellular redox demands during industrial applications.
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