| 纯度 | >95%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | RAGE |
| Uniprot No | Q62151-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-342aa |
| 氨基酸序列 | MPAGTAARAW VLVLALWGAV AGGQNITARI GEPLVLSCKG APKKPPQQLE WKLNTGRTEA WKVLSPQGGP WDSVARILPN GSLLLPATGI VDEGTFRCRA TNRRGKEVKS NYRVRVYQIP GKPEIVDPAS ELTASVPNKV GTCVSEGSYP AGTLSWHLDG KLLIPDGKET LVKEETRRHP ETGLFTLRSE LTVIPTQGGT HPTFSCSFSL GLPRRRPLNT APIQLRVREP GPPEGIQLLV EPEGGIVAPG GTVTLTCAIS AQPPPQVHWI KDGAPLPLAP SPVLLLPEVG HEDEGTYSCV ATHPSHGPQE SPPVSIRVTE TGDEGPAEGS VGESGLGTLA LA |
| 预测分子量 | 35 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3篇关于RAGE重组蛋白的虚构参考文献示例(仅供格式参考)：
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1. **标题**: *Expression and structural characterization of human RAGE extracellular domain in E. coli*
**作者**: Smith A, et al.
**摘要**: 报道了在大肠杆菌中高效表达可溶性人源RAGE胞外域重组蛋白的方法，并通过X射线晶体学解析其三维结构，揭示了与配体结合的关键结构域。
2. **标题**: *RAGE recombinant protein exacerbates inflammatory response in diabetic mouse models*
**作者**: Chen L, et al.
**摘要**: 利用重组RAGE蛋白干预糖尿病小鼠模型，发现其通过激活NF-κB通路增强炎症反应，提示RAGE在糖尿病并发症中的病理作用。
3. **标题**: *Development of a RAGE-ligand binding inhibitor based on recombinant chimeric protein design*
**作者**: Tanaka K, et al.
**摘要**: 构建了一种嵌合型RAGE重组蛋白，通过阻断AGEs(晚期糖基化终产物)与RAGE的结合，显著减轻了动脉粥样硬化模型中的血管损伤。
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注：以上文献为示例性质，实际引用请通过PubMed或学术数据库检索真实文献(如搜索关键词：RAGE recombinant protein, sRAGE expression)。
**Background of RAGE Recombinant Protein**
The Receptor for Advanced Glycation End-products (RAGE) is a transmembrane protein belonging to the immunoglobulin superfamily, initially identified as a receptor for advanced glycation end-products (AGEs). These AGEs are harmful compounds formed through non-enzymatic glycation reactions, particularly under hyperglycemic or oxidative stress conditions. Beyond AGEs, RAGE interacts with diverse ligands, including high-mobility group box 1 (HMGB1), S100/calgranulins, and amyloid-β, positioning it as a key player in chronic inflammation, oxidative stress, and cellular dysfunction.
RAGE activation triggers downstream signaling pathways, such as NF-κB and MAPK, which drive pro-inflammatory cytokine production and sustain pathological processes. Its involvement in diabetes complications, atherosclerosis, neurodegenerative disorders (e.g., Alzheimer’s disease), and cancer metastasis has made RAGE a focal point in biomedical research. However, studying RAGE’s native form in biological systems is challenging due to low baseline expression and complex ligand interactions.
Recombinant RAGE proteins, produced via genetic engineering in systems like *E. coli* or mammalian cells, offer a solution. These purified proteins retain functional domains (e.g., ligand-binding V-type domain) and are critical for *in vitro* studies, structural analyses, and drug screening. Researchers use them to map ligand-binding interfaces, elucidate signaling mechanisms, and develop therapeutic inhibitors (e.g., soluble RAGE decoys or monoclonal antibodies). Additionally, recombinant RAGE serves as an antigen for antibody development or diagnostic tools in disease models.
Despite progress, questions remain about isoform-specific functions, post-translational modifications, and context-dependent roles in disease. Ongoing research aims to refine recombinant RAGE applications for targeted therapies and biomarker discovery.
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