| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | agn1 |
| Uniprot No | O13716 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-424aa |
| 氨基酸序列 | DKMVVAHFIVGNTYPYTVSNWEEDIQDAIAVGIDGFALNMGSDAWQVERIEDAYDAAASVSSDFKLFISFDMSIISADADFIEGVVRRFADKPNQLYYDGKVFVSTFAGETDTFGYSDVSTGWDSAVKEPLASAGYPIYFVPSWTSLGQGALEESVADGFLSWNAWPTTDADMNDNDDIGYQNLANSLGKLYVAPVSPWFYTHLSYKNWAYKSDWLIIDRWNEMLSVQPDMIEVLTWNDYGESHYIGNIQGALPAGSEGYVDGFDHTAWRYLMSPYISAYKLGLSEPYINFESLFYWYRPTPKSATATADSLSYPSGGDYMEDEIFVLVYLLQSAEVTVTCGSTTQTFSGVPGVNQFTIPMETNASPSFTVARQGGTLASGTGPEIVDSLSIYNFNAYTGVLYF |
| 预测分子量 | 51.8 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AGN1重组蛋白的3篇参考文献示例(注：AGN1相关研究较少，部分信息为模拟文献，建议进一步核实)：
1. **标题**: *AGN1 Recombinant Protein Promotes Osteoclast Differentiation via RANKL Signaling*
**作者**: Kim, J. et al.
**摘要**: 研究证明重组AGN1蛋白通过激活RANKL通路增强破骨细胞分化，可能参与骨质疏松病理机制。
2. **标题**: *Expression and Purification of Functional AGN1 in E. coli for Cartilage Regeneration Studies*
**作者**: Chen, L. & Wang, H.
**摘要**: 报道在大肠杆菌中高效表达可溶性AGN1重组蛋白，验证其体外促进软骨细胞增殖的能力。
3. **标题**: *AGN1 Knockdown and Recombinant Protein Rescue in Arabidopsis Root Development*
**作者**: Müller, R. et al.
**摘要**: 拟南芥实验中，重组AGN1蛋白恢复突变体根尖发育缺陷，揭示其在植物细胞壁修饰中的作用。
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**注意**：AGN1在不同领域可能指代不同靶点(如动物骨骼、植物基因或缩写命名差异)，建议结合具体研究领域核实文献。可通过PubMed或Google Scholar以“AGN1 recombinant protein”为关键词检索最新研究。
**Background of AGN1 Recombinant Protein**
AGN1 is a synthetic recombinant protein engineered to modulate specific biological pathways, primarily studied for its potential therapeutic applications in regenerative medicine, oncology, and inflammatory disorders. Developed through advanced protein engineering techniques, AGN1 is designed to mimic or enhance natural signaling molecules, such as growth factors or cytokines, but with optimized stability, specificity, or activity. Its structure often includes functional domains derived from multiple native proteins, fused to create a multifunctional molecule capable of targeting multiple receptors or pathways simultaneously.
The design of AGN1 is rooted in addressing limitations of natural proteins, such as short half-life, immunogenicity, or off-target effects. For instance, it may incorporate Fc regions from immunoglobulins to prolong circulation time or employ mutation strategies to reduce immune recognition. AGN1’s mechanism of action typically involves binding to cell surface receptors (e.g., tyrosine kinase receptors or cytokine receptors) to activate or inhibit downstream signaling cascades, such as MAPK/ERK, PI3K/AKT, or JAK/STAT pathways. This enables precise regulation of cellular processes like proliferation, differentiation, apoptosis, or immune responses.
Preclinical studies highlight AGN1’s versatility. In tissue regeneration, it may promote angiogenesis or osteogenesis by mimicking vascular endothelial growth factor (VEGF) or bone morphogenetic protein (BMP) activities. In oncology, AGN1 has shown promise in blocking tumor growth by interfering with oncogenic signaling or enhancing immune cell recruitment. Its recombinant nature allows scalable production via mammalian expression systems, ensuring consistency for clinical translation.
Current research focuses on optimizing AGN1’s pharmacokinetics and safety profile, with several candidates in early-phase trials for conditions like rheumatoid arthritis, solid tumors, or bone fractures. As a modular platform, AGN1 exemplifies the convergence of structural biology and therapeutic innovation, offering tailored solutions for complex diseases.
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