| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NGRN |
| Uniprot No | Q9NPE2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-291aa |
| 氨基酸序列 | AVTRC GFATRGVAGP GPIGREPDPD SDWEPEEREL QEVESTLKRQ KQAIRFQKIR RQMEAPGAPP RTLTWEAMEQ IRYLHEEFPE SWSVPRLAEG FDVSTDVIRR VLKSKFLPTL EQKLKQDQKV LKKAGLAHSL QHLRGSGNTS KLLPAGHSVS GSLLMPGHEA SSKDPNHSTA LKVIESDTHR TNTPRRRKGR NKEIQDLEES FVPVAAPLGH PRELQKYSSD SESPRGTGSG ALPSGQKLEE LKAEEPDNFS SKVVQRGREF FDSNGNFLYR I |
| 预测分子量 | 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NGRN重组蛋白的3篇示例参考文献(注：NGRN相关研究较少，以下为模拟文献示例，实际引用请以真实文献为准)：
1. **文献名称**：Expression and Purification of Recombinant NGRN Protein in E. coli
**作者**：Zhang Y, et al.
**摘要**：本研究成功构建了NGRN基因的重组质粒，并利用大肠杆菌表达系统实现了高效表达。通过亲和层析纯化获得高纯度蛋白，Western blot验证其抗原性，为后续功能研究奠定基础。
2. **文献名称**：Structural Characterization of NGRN and Its Role in Cell Proliferation
**作者**：Lee SJ, Kim H.
**摘要**：采用X射线晶体学解析了NGRN蛋白的三维结构，发现其具有独特的受体结合域。体外实验表明，重组NGRN可促进特定肿瘤细胞系的增殖，提示其潜在信号通路调控作用。
3. **文献名称**：NGRN Recombinant Protein as a Novel Therapeutic Target in Ischemic Injury
**作者**：Wang X, et al.
**摘要**：通过哺乳动物细胞表达系统制备功能性NGRN重组蛋白，动物实验证实其可减轻缺血再灌注损伤模型的炎症反应，机制可能与调控NF-κB通路相关，具有治疗潜力。
提示：若需真实文献，建议在PubMed/Google Scholar以"NGRN recombinant protein"为关键词检索，并筛选近年研究。部分文献可能涉及NGRN基因功能或重组技术优化方向。
**Background of NGRN Recombinant Protein**
NGRN (Neurogranin) is a small, calmodulin-binding protein predominantly expressed in the brain, particularly in dendritic spines and postsynaptic terminals. It plays a critical role in synaptic plasticity, learning, and memory by modulating calcium-mediated signaling pathways. Neurogranin interacts with calmodulin, regulating its availability and influencing downstream targets like calcium/calmodulin-dependent protein kinase II (CaMKII), which is essential for long-term potentiation (LTP). Dysregulation of NGRN has been linked to neurodegenerative disorders, including Alzheimer’s disease, where reduced cerebrospinal fluid (CSF) levels correlate with cognitive decline, positioning it as a potential biomarker.
Recombinant NGRN protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for research. Its recombinant form retains the ability to bind calmodulin and mimic native protein interactions, enabling studies on synaptic mechanisms, calcium signaling, and disease pathology. Researchers utilize NGRN recombinant protein in *in vitro* assays, structural studies, and therapeutic development. It also serves as an antigen for antibody production in diagnostic kits.
The development of recombinant NGRN addresses challenges in sourcing native protein from biological tissues, ensuring consistency, scalability, and reduced batch variability. Its applications span neuroscience, drug discovery, and biomarker validation, underscoring its importance in understanding and targeting synaptic dysfunction in neurological diseases.
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