| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSN |
| Uniprot No | P06396 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 514-782aa |
| 氨基酸序列 | DEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA |
| 预测分子量 | 33.5 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GSN(gelsolin)重组蛋白的3篇示例文献(内容为假设性概括，实际文献需通过学术数据库检索)：
1. **《高效表达可溶性人源gelsolin重组蛋白的大肠杆菌系统优化》**
- 作者：Zhang Y, Wang L, et al.
- 摘要：研究通过密码子优化和表达条件调控，在大肠杆菌中实现了人源GSN重组蛋白的可溶性高效表达，为大规模生产提供方案。
2. **《重组gelsolin蛋白在败血症模型中的抗炎作用研究》**
- 作者：Lee S, Chen X, et al.
- 摘要：利用真核表达系统制备重组GSN蛋白，证明其通过结合炎性因子(如LPS)显著减轻小鼠败血症症状，提示临床治疗潜力。
3. **《基于哺乳动物细胞表达的重组gelsolin的糖基化修饰与功能分析》**
- 作者：Smith J, Brown K, et al.
- 摘要：对比不同表达系统生产的GSN蛋白，发现哺乳动物细胞表达的糖基化修饰版本在细胞凋亡调控中活性更高，强调了翻译后修饰的重要性。
**备注**：以上为示例，真实文献建议通过PubMed或Web of Science搜索关键词“recombinant gelsolin protein”获取，并关注近5-10年高被引研究。
Gelsolin (GSN), a multifunctional actin-binding protein, plays pivotal roles in cytoskeletal remodeling, cell motility, and inflammation regulation. Initially identified as a cytoplasmic protein, it exists in two isoforms: cytoplasmic (cGSN) and plasma (pGSN), the latter secreted into blood. GSN modulates actin dynamics by severing, capping, or nucleating actin filaments, influencing cellular processes like wound healing, immune response, and apoptosis. Its depletion or dysfunction is linked to amyloidosis, cancer metastasis, and neurodegenerative diseases.
Recombinant GSN (rGSN) is produced using heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to study its structure-function relationships or therapeutic potential. Bacterial systems offer cost-effective yields but lack post-translational modifications, whereas eukaryotic systems better mimic native protein properties. Purification typically involves affinity chromatography, leveraging tags like His-tag.
Research highlights rGSN’s therapeutic promise. In sepsis, exogenous rGSN neutralizes pro-inflammatory mediators (e.g., LPS) and clears actin filaments released during tissue injury, mitigating systemic inflammation. Preclinical studies show efficacy in reducing mortality in septic models. It also demonstrates antifibrotic activity by inhibiting TGF-β signaling and attenuating extracellular matrix deposition. Additionally, rGSN’s actin-scavenging capacity protects against ischemic injury in stroke or myocardial infarction models.
Despite progress, challenges persist. Large-scale production requires optimizing expression systems for stability and bioactivity. Immunogenicity concerns necessitate humanized expression platforms. Drug delivery hurdles, including short plasma half-life, demand formulation innovations like PEGylation or nanoparticle encapsulation. Ongoing studies explore engineered variants with enhanced therapeutic profiles. As a biomarker, rGSN aids in diagnosing inflammatory or degenerative conditions, underscoring its dual diagnostic-therapeutic value in precision medicine.
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