| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | GNaO1 |
| Uniprot No | P18872 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-354aa |
| 氨基酸序列 | GCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKTDSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAGDYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY |
| 预测分子量 | 42.0 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GNAO1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *"Heterologous Expression and Purification of GNAO1 in Escherichia coli for Structural Studies"*
**作者**: Smith J, et al.
**摘要**: 该研究报道了通过大肠杆菌系统高效表达并纯化人源GNAO1重组蛋白的方法，利用X射线晶体学解析其三维结构，为研究G蛋白α亚基的构象变化提供基础。
2. **文献名称**: *"Functional Characterization of GNAO1 Mutants Associated with Neurodevelopmental Disorders"*
**作者**: Tanaka K, et al.
**摘要**: 作者通过重组GNAO1蛋白体外实验，揭示致病性突变(如p.Gly203Arg)导致Gαo蛋白GTP酶活性异常，进而扰乱cAMP信号通路，解释了其与癫痫和运动障碍的关联机制。
3. **文献名称**: *"Interaction between Recombinant GNAO1 and RIC8A: Insights into G Protein Signaling Regulation"*
**作者**: Garcia-Reyes MA, et al.
**摘要**: 研究利用重组GNAO1蛋白与伴侣蛋白RIC8A的共纯化实验，证明RIC8A通过稳定Gαo的活性构象增强其信号转导效率，为神经细胞中G蛋白偶联受体调控提供新证据。
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(注：以上文献为虚拟示例，实际研究中建议通过PubMed或Web of Science检索具体文章。)
GNaO1. also known as Guanine Nucleotide-binding Protein G(o) Subunit Alpha-1. is a critical component of heterotrimeric G proteins involved in intracellular signal transduction. Encoded by the *GNAO1* gene, this protein belongs to the Gαo subclass of Gα subunits, which are pivotal for modulating neurotransmitter release, ion channel activity, and synaptic plasticity in the central nervous system (CNS). GNaO1 is predominantly expressed in neuronal tissues, where it couples with G protein-coupled receptors (GPCRs) to regulate downstream effectors such as adenylyl cyclase, calcium channels, and mitogen-activated protein kinase (MAPK) pathways.
Mutations in *GNAO1* are linked to severe neurodevelopmental disorders, including early infantile epileptic encephalopathy (EIEE17) and movement disorders characterized by dystonia, chorea, and developmental delay. These pathogenic variants often disrupt GTPase activity or impair receptor interactions, leading to dysregulated signaling cascades. Recombinant GNaO1 protein is engineered in vitro using expression systems like *E. coli* or mammalian cells to study its structure-function relationships, mutation-driven pathologies, and interaction networks. Researchers employ techniques such as affinity chromatography and tag-based purification (e.g., His-tag) to obtain high-purity protein for biochemical assays, crystallography, or drug screening.
The recombinant protein serves as a vital tool for elucidating disease mechanisms and developing targeted therapies. For instance, it aids in screening small molecules that restore normal GTPase activity or stabilize mutant conformations. Additionally, structural studies using recombinant GNaO1 have revealed insights into its helical domain organization and GTP-binding pocket, informing precision medicine approaches. As *GNAO1*-related disorders lack curative treatments, recombinant protein-based research remains a cornerstone for advancing diagnostic and therapeutic innovations in neurogenetics.
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