| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLO1 |
| Uniprot No | Q04760 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYT RVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLE LTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFV KKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM |
| 预测分子量 | 21 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GLO1(Glyoxalase 1)重组蛋白的3篇参考文献示例，内容基于真实研究概括，但具体作者和标题可能与实际文献略有差异，建议通过学术数据库核实：
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1. **文献名称**: *"Recombinant expression and characterization of human glyoxalase I in Escherichia coli"*
**作者**: Thornalley PJ, et al.
**摘要**: 研究报道了人源GLO1基因在大肠杆菌中的重组表达与纯化，验证了其酶活性对甲基乙二醛的解毒功能，并探讨了重组蛋白在糖尿病并发症模型中的潜在应用。
2. **文献名称**: *"Crystal structure of recombinant human glyoxalase I: insights into substrate specificity"*
**作者**: Bito A, et al.
**摘要**: 通过X射线晶体学解析了重组人GLO1的三维结构，揭示了其催化活性位点的关键氨基酸残基，并阐明了其特异性识别甲基乙二醛的分子机制。
3. **文献名称**: *"Glyoxalase I overexpression in cancer cells: recombinant protein studies on drug resistance"*
**作者**: Kawatani M, et al.
**摘要**: 利用重组GLO1蛋白研究其在癌细胞中的高表达现象，发现其通过降低毒性代谢物水平增强肿瘤细胞对化疗药物的耐药性，为靶向GLO1的抗癌策略提供依据。
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**注意**：以上为模拟摘要，实际文献请通过PubMed、Google Scholar等平台检索关键词(如"recombinant GLO1 protein" "glyoxalase I expression")获取准确信息。
**Background of GLO1 Recombinant Protein**
Glyoxalase I (GLO1) is a critical enzyme within the glyoxalase system, a metabolic pathway responsible for detoxifying methylglyoxal (MG), a highly reactive α-ketoaldehyde generated as a byproduct of glycolysis. MG accumulation leads to the formation of advanced glycation end-products (AGEs), which contribute to cellular damage, oxidative stress, and inflammation. GLO1 catalyzes the isomerization of the MG-glutathione hemithioacetal adduct to S-D-lactoylglutathione, a less toxic metabolite, thereby protecting cells from MG-induced cytotoxicity. This enzyme plays a vital role in maintaining cellular homeostasis and has been implicated in various pathologies, including diabetes, cancer, neurodegenerative diseases, and aging.
Recombinant GLO1 protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. Its production enables large-scale, high-purity yields for research and therapeutic applications. Recombinant GLO1 retains the enzymatic activity of native GLO1. making it valuable for studying MG metabolism, AGE-related mechanisms, and oxidative stress pathways. It is also utilized in drug discovery to screen for modulators of GLO1 activity, as enhancing its function could mitigate MG-associated diseases.
Recent studies highlight GLO1's potential as a therapeutic target. For instance, GLO1 upregulation has been linked to improved insulin sensitivity in diabetes, while its downregulation in cancer cells may sensitize them to chemotherapy. However, its role remains context-dependent, necessitating further exploration. The availability of recombinant GLO1 facilitates structural studies, enzyme kinetics analyses, and preclinical evaluations, advancing our understanding of its physiological and pathological significance. Overall, GLO1 recombinant protein serves as a key tool in both basic research and translational medicine, offering insights into disease mechanisms and therapeutic strategies.
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