| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCNN1g |
| Uniprot No | P51170 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-649aa |
| 氨基酸序列 | MAPGEKIKAKIKKNLPVTGPQAPTIKELMRWYCLNTNTHGCRRIVVSRGRLRRLLWIGFTLTAVALILWQCALLVFSFYTVSVSIKVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQETREALKSLYGFPESRKRREAESWNSVSEGKQPRFSHRIPLLIFDQDEKGKARDFFTGRKRKVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNRENETILSTSMGGSEYGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMVTSIGMHLTESFKLSEPYSQCTEDGSDVPIRNIYNAAYSLQICLHSCFQTKMVEKCGCAQYSQPLPPAANYCNYQQHPNWMYCYYQLHRAFVQEELGCQSVCKEACSFKEWTLTTSLAQWPSVVSEKWLLPVLTWDQGRQVNKKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMSCSVVCVIEIIEVFFIDFFSIIARRQWQKAKEWWAWKQAPPCPEAPRSPQGQDNPALDIDDDLPTFNSALHLPPALGTQVPGTPPPKYNTLRLERAFSNQLTDTQMLDEL |
| 预测分子量 | 74,2 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SCNN1g重组蛋白的3篇代表性文献信息(注：部分内容为模拟示例，实际文献需根据具体研究检索)：
1. **文献名称**: "Functional expression and purification of the human epithelial sodium channel gamma subunit (SCNN1G) in a heterologous system"
**作者**: Smith J, et al.
**摘要**: 该研究成功在昆虫细胞中表达并纯化了人源SCNN1g重组蛋白，通过电生理学实验证实其与α、β亚基共同组装形成功能性上皮钠通道，并分析了其离子选择性特征。
2. **文献名称**: "Structural insights into the γ subunit of the epithelial sodium channel using recombinant protein crystallography"
**作者**: Chen L, et al.
**摘要**: 利用大肠杆菌表达系统获得高纯度SCNN1g重组蛋白，通过X射线晶体学解析其胞外结构域的三维结构，揭示了与盐敏感性高血压相关的突变位点的空间构象。
3. **文献名称**: "SCNN1G recombinant protein modulates airway surface liquid viscosity in cystic fibrosis models"
**作者**: Wang Y, et al.
**摘要**: 研究通过哺乳动物细胞表达SCNN1g重组蛋白，证明其在囊性纤维化体外模型中调节气道表面液体黏度的功能，为靶向ENaC的药物治疗提供实验依据。
**提示**：实际文献需通过PubMed/Google Scholar检索关键词“SCNN1G recombinant”“ENaC gamma subunit expression”等获取。部分研究可能侧重于亚基复合物而非单一重组蛋白，建议结合具体研究方向筛选。
The SCNN1g gene encodes the gamma subunit of the epithelial sodium channel (ENaC), a critical ion channel involved in sodium absorption and fluid homeostasis. ENaC, composed of α, β, and γ subunits (SCNN1a, SCNN1b, SCNN1g), is primarily expressed in epithelial tissues such as the kidneys, lungs, and colon. It facilitates passive sodium transport across apical membranes, regulated by aldosterone and vasopressin, playing a pivotal role in blood pressure regulation, airway surface liquid maintenance, and electrolyte balance. Dysregulation of ENaC activity is linked to diseases like Liddle syndrome (hypertension due to hyperactive channels), pseudohypoaldosteronism (salt-wasting disorders), and cystic fibrosis-related complications.
Recombinant SCNN1g protein is engineered using expression systems (e.g., mammalian or insect cells) to produce the gamma subunit for functional and structural studies. Its production enables researchers to explore ENaC assembly, activation mechanisms, and interactions with regulatory proteins or drugs. For example, studies using recombinant SCNN1g have clarified how mutations alter channel kinetics or contribute to sodium retention in hypertension. Additionally, it serves as a tool for screening ENaC inhibitors, such as amiloride analogs, which are investigated for treating conditions like cystic fibrosis or hypertension.
The protein’s structure includes two transmembrane domains, a large extracellular loop, and intracellular N- and C-termini. Post-translational modifications (e.g., glycosylation) in recombinant SCNN1g are often preserved to mimic native protein behavior. Challenges in production include maintaining subunit stoichiometry and membrane localization. Recent advances in cryo-EM and electrophysiological assays using recombinant SCNN1g have provided high-resolution insights into ENaC gating and regulatory mechanisms, driving therapeutic innovations. Overall, recombinant SCNN1g is indispensable for understanding ENaC biology and developing targeted therapies for sodium-related disorders.
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