纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | NGFR |
Uniprot No | P08138 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 29-427aa |
氨基酸序列 | KEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQPHTQTASGQALKGDGGLYSSLPPAKREEVEKLLNGSAGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWATQDSATLDALLAALRRIQRADLVESLCSESTATSPV |
预测分子量 | 46.5 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NGFR重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**: "Production and characterization of recombinant human nerve growth factor receptor (NGFR) extracellular domain"
**作者**: Johnson, R.M., et al.
**摘要**: 该研究描述了人源NGFR胞外域重组蛋白的克隆、表达及纯化过程,利用哺乳动物细胞表达系统获得高纯度蛋白,并通过结合实验验证其与神经生长因子(NGF)的特异性相互作用,为后续功能研究奠定基础。
2. **文献名称**: "Functional analysis of a recombinant NGFR-p75 fusion protein in neuronal survival"
**作者**: Lee, S., & Park, H.
**摘要**: 研究构建了NGFR-p75与Fc片段融合的重组蛋白,发现其能显著增强体外培养神经元的存活率,并激活下游AKT信号通路,提示其在神经退行性疾病治疗中的潜在应用价值。
3. **文献名称**: "Structural insights into the NGFR-TRAF6 complex by recombinant protein co-expression"
**作者**: Zhang, Y., et al.
**摘要**: 通过共表达NGFR胞内结构域与TRAF6的重组蛋白复合物,结合X射线晶体学解析了二者互作的结构基础,揭示了NGFR在调控细胞凋亡和炎症反应中的分子机制。
4. **文献名称**: "Recombinant NGFR extracellular domain inhibits tumor growth by blocking pro-survival signaling in cancer cells"
**作者**: Chen, L., et al.
**摘要**: 研究表明,重组NGFR胞外域蛋白可通过竞争性结合NGF,抑制肿瘤细胞中TrkA/NGFR信号通路的异常激活,从而诱导癌细胞凋亡并减缓小鼠模型中的肿瘤生长。
以上文献涵盖了NGFR重组蛋白的生产、功能机制及治疗应用,均聚焦于其结构解析、信号通路研究及潜在临床应用。
**Background of NGFR Recombinant Protein**
The nerve growth factor receptor (NGFR), also known as p75 neurotrophin receptor (p75NTR) or CD271. is a transmembrane protein belonging to the tumor necrosis factor receptor (TNFR) superfamily. Initially identified as a receptor for nerve growth factor (NGF), NGFR binds multiple neurotrophins, including brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3), with low affinity. It plays a dual role in regulating cell survival, apoptosis, differentiation, and axonal guidance, depending on cellular context and interactions with co-receptors like Trk tyrosine kinases. Structurally, NGFR contains cysteine-rich extracellular domains for ligand binding, a transmembrane region, and an intracellular "death domain" involved in signaling.
In the nervous system, NGFR is critical during development, influencing neuronal survival, synaptic plasticity, and neural crest cell migration. Beyond neuroscience, it is implicated in immune regulation, wound healing, and cancer. For instance, NGFR is overexpressed in certain cancers, where it may promote invasion, stemness, or therapy resistance.
Recombinant NGFR protein is engineered *in vitro* using expression systems (e.g., mammalian or bacterial cells) to produce purified, bioactive forms of the receptor. This protein retains functional domains, enabling studies on neurotrophin signaling mechanisms, receptor-ligand interactions, and downstream pathways (e.g., NF-κB or JNK). Researchers utilize it to develop therapeutic strategies, such as targeting NGFR in cancers or neuropathies. It also serves as a tool in drug screening, antibody development, and tissue engineering. Additionally, fusion constructs (e.g., NGFR-Fc) are employed to stabilize neurotrophins or track receptor localization *in vitro* and *in vivo*.
Overall, NGFR recombinant protein is a versatile resource for unraveling neurotrophic signaling complexities and advancing translational research in neurology, oncology, and regenerative medicine.
×