| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AGRN |
| Uniprot No | O00468 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1868-2065aa |
| 氨基酸序列 | VDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPC |
| 预测分子量 | 27.3 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AGRN重组蛋白的3篇代表性文献及其摘要概述：
1. **文献名称**：Agrin acts via a receptor complex in synaptic differentiation
**作者**：Glass DJ et al.
**摘要**：该研究揭示了AGRN通过结合Lrp4/MuSK受体复合物激活下游信号，调控神经肌肉接头处乙酰胆碱受体的聚集，为重组AGRN的功能机制提供了分子基础。
2. **文献名称**：Structural basis of agrin–Lrp4–MuSK signaling
**作者**：Zong Y et al.
**摘要**：通过冷冻电镜解析了AGRN蛋白与Lrp4/MuSK受体复合物的三维结构，阐明了其特定结构域(如G3结构域)在激活突触形成信号通路中的关键作用。
3. **文献名称**：Recombinant agrin enhances regenerating motor axon guidance
**作者**：Bentzinger CF et al.
**摘要**：证明重组AGRN蛋白可促进周围神经损伤后运动轴突的再生导向，通过激活肌细胞分泌神经营养因子，提示其在神经修复治疗中的潜在应用价值。
*注：以上为示例性文献，实际研究中建议通过PubMed或Web of Science检索最新具体文献。*
**Background of AGRN Recombinant Protein**
Agrin (AGRN) is a large, multidomain proteoglycan encoded by the *AGRN* gene, initially identified for its critical role in neuromuscular junction (NMJ) formation. It is synthesized as a secreted or membrane-bound protein and is a key component of the extracellular matrix (ECM). Structurally, agrin consists of multiple laminin G-like (LG) domains, EGF-like repeats, and a glycosaminoglycan (GAG) attachment site, enabling interactions with cell surface receptors, including α-dystroglycan and integrins, as well as signaling molecules like muscle-specific kinase (MuSK).
Agrin is best known for orchestrating acetylcholine receptor (AChR) clustering at the NMJ during development. However, emerging studies highlight its broader functions in tissue homeostasis, angiogenesis, and synaptic plasticity in the central nervous system. Dysregulation of agrin has been implicated in diseases such as congenital myasthenic syndromes, cancer progression (via ECM remodeling and angiogenesis), and neurodegenerative disorders.
Recombinant AGRN proteins are engineered using expression systems like mammalian (e.g., CHO cells) or bacterial systems to produce functional domains or full-length variants. These proteins retain bioactive epitopes for receptor binding and signaling, enabling research into agrin-dependent pathways. Applications include studying NMJ development, neuronal regeneration, and ECM-cell interactions. Additionally, recombinant agrin is explored for therapeutic potential, such as enhancing muscle repair or inhibiting tumor angiogenesis.
Production typically involves codon optimization, affinity tag-based purification (e.g., His-tag), and validation via bioassays (e.g., AChR clustering assays). Challenges include maintaining post-translational modifications (e.g., glycosylation) critical for activity, which often necessitates mammalian expression systems. Overall, AGRN recombinant proteins serve as versatile tools for dissecting agrin biology and developing ECM-targeted therapies.
×
