| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AGE |
| Uniprot No | P51606 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-427aa |
| 氨基酸序列 | MSKGLPARQDMEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGRQVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMAVPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCLGRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADNFCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFGYLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE |
| 预测分子量 | 48,8 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AGE重组蛋白的3篇模拟参考文献，格式为文献名称、作者及摘要概述：
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1. **文献名称**: *Recombinant Expression and Characterization of Advanced Glycation End-Product (AGE) Modified Proteins in vitro*
**作者**: Smith A, et al.
**摘要**: 研究通过大肠杆菌系统重组表达人源AGE修饰蛋白，优化了体外糖基化反应条件，验证了其与RAGE受体的结合活性，为研究AGE在糖尿病并发症中的作用提供工具。
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2. **文献名称**: *Engineered AGE-BSA Recombinant Protein as a Model for Studying Cellular Oxidative Stress*
**作者**: Zhang Y, et al.
**摘要**: 构建了AGE修饰的牛血清白蛋白(AGE-BSA)重组蛋白模型，证实其可诱导内皮细胞氧化应激和炎症因子释放，揭示了AGE在动脉粥样硬化中的潜在机制。
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3. **文献名称**: *Inhibitory Effects of Recombinant AGE-Breaker Proteins on Diabetic Nephropathy in Rats*
**作者**: Tanaka K, et al.
**摘要**: 设计了一种重组AGE裂解酶蛋白，并在糖尿病大鼠模型中验证其能有效降解肾脏AGE沉积，改善肾功能，为治疗糖尿病肾病提供新策略。
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注：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
**Background of AGE Recombinant Proteins**
Advanced Glycation End-products (AGEs) are heterogeneous compounds formed through non-enzymatic glycation reactions between reducing sugars and proteins, lipids, or nucleic acids. These modifications accumulate naturally with aging and are exacerbated in metabolic disorders like diabetes, contributing to tissue dysfunction and chronic diseases. To study AGE-related mechanisms or develop therapeutic interventions, researchers often employ recombinant proteins modified to mimic or interact with AGEs.
AGE recombinant proteins are typically engineered using recombinant DNA technology, where target proteins (e.g., receptors like RAGE or enzymes like glyoxalase-1) are expressed in host systems like *E. coli*, yeast, or mammalian cells. These proteins enable precise investigation of AGE-receptor interactions, signaling pathways (e.g., NF-κB activation), or degradation processes. For example, recombinant RAGE is used to screen inhibitors of AGE-RAGE binding, while recombinant glyoxalase-1 helps explore detoxification of reactive carbonyl precursors of AGEs.
Applications span biomedical research, diagnostics, and drug development. AGE-modified recombinant albumin or collagen serves as standardized tools to model diabetic complications or aging in vitro. In therapeutics, recombinant enzymes or antibodies targeting AGEs are being tested to mitigate diabetic nephropathy, retinopathy, or neurodegenerative diseases.
Challenges include ensuring proper post-translational modifications in host systems and replicating the structural complexity of endogenous AGEs. Despite this, AGE recombinant proteins remain vital for unraveling AGE biology and advancing anti-AGE strategies, bridging gaps between biochemical research and clinical translation.
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