| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | SPG |
| Uniprot No | P19909 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 291-497aa |
| 氨基酸序列 | IDEILAALPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE |
| 预测分子量 | 26.6 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3条关于SPG重组蛋白的模拟参考文献，供参考：
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1. **文献名称**：*Functional Characterization of SPG4 (Spastin) Recombinant Protein in Microtubule Severing*
**作者**：Salinas S. et al.
**摘要**：本研究通过体外重组表达了人源SPG4蛋白(spastin)，并验证其微管切割活性。实验表明，spastin的ATP酶结构域对其调控神经元轴突微管动态平衡至关重要，突变体导致功能缺陷，解释了遗传性痉挛性截瘫的病理机制。
2. **文献名称**：*Expression and Purification of SPG11 Recombinant Protein for Neuronal Function Analysis*
**作者**：Martinez-Carrera L.A., Wirth B.
**摘要**：文章报道了一种高效表达并纯化SPG11(spatacsin)重组蛋白的方法。通过细胞模型发现，SPG11缺失会导致溶酶体运输异常，提示其在维持神经元内吞通路中的关键作用，为SPG11相关疾病的治疗提供靶点。
3. **文献名称**：*Structural Insights into SPG3A (Atlastin-1) Recombinant Protein Using Cryo-EM*
**作者**：Zhu P.P., Blackstone C.
**摘要**：利用冷冻电镜解析了SPG3A编码的Atlastin-1重组蛋白的三维结构，揭示了其介导内质网膜融合的分子机制。突变分析表明，结构域稳定性丧失与早发型痉挛性截瘫的发病密切相关。
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**注**：以上文献为示例性内容，实际引用需以真实发表的论文为准。建议通过PubMed、Google Scholar等平台以“SPG recombinant protein”或具体基因名(如SPG4、SPG11)为关键词检索最新研究。
Streptococcal protein G (SPG) is a bacterial cell wall protein originally isolated from *Streptococcus* species, notably Group C and G streptococci. It gained prominence due to its ability to bind immunoglobulins (IgG), similar to *Staphylococcus* Protein A, but with broader species specificity. Naturally occurring Protein G contains multiple domains, including IgG-binding regions that interact with the Fc portion of antibodies and albumin-binding regions. However, recombinant versions of Protein G (rProtein G) are engineered to eliminate non-essential domains (e.g., albumin-binding sites) while retaining optimized IgG-binding functionality, enhancing its utility in biotechnological applications.
Recombinant Protein G is widely employed in antibody purification, immunodetection, and diagnostic assays due to its high affinity for IgG subclasses across diverse species, including human, mouse, and rabbit. Unlike Protein A, it effectively binds IgG3 (in humans) and antibodies from rodents, making it indispensable in monoclonal antibody production and research. Its recombinant form is typically expressed in *E. coli* or other host systems, ensuring scalability and cost-effectiveness. Modern variants may also include tags (e.g., His-tags) for simplified purification or immobilization.
The development of recombinant Protein G revolutionized antibody-based technologies by offering improved stability, reduced non-specific binding, and adaptability to industrial workflows. Its applications span affinity chromatography, ELISA, flow cytometry, and therapeutic antibody manufacturing. Ongoing engineering efforts continue to refine its binding kinetics and compatibility with synthetic platforms, solidifying its role as a cornerstone reagent in both academic and biopharmaceutical settings.
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