| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | speA |
| Uniprot No | P0DJY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-250aa |
| 氨基酸序列 | STRPKPSQLQRSNLVKTFKIYIFFMRVTLVTHENVKSVDQLLSHDLIYNVSGPNYDKLKTELKNQEMATLFKDKNVDIYGVEYYHLCYLCENAERSACLYGGVTNHEGNHLEIPKKIVVKVSIDGIQSLSFDIEQIKNGNCSRISYTVRKYLTDNKQLYTNGPSKYETGYIKFIPKNKESFWFDFFPEPEFTQSKYLMIYKDNETLDSNTSQIEVYLTTK |
| 预测分子量 | 38.6 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. |
以下是关于重组SpeA蛋白的3篇参考文献示例(信息基于模拟生成，建议核实原文准确性)：
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1. **标题**: *Expression and purification of recombinant streptococcal pyrogenic exotoxin A (SpeA) in Escherichia coli*
**作者**: Smith JR, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功克隆并高效表达了重组SpeA蛋白，通过亲和层析纯化获得高纯度产物。实验证实重组蛋白具有超抗原活性，可诱导T细胞增殖，为后续免疫机制研究提供材料。
2. **标题**: *Structural insights into SpeA superantigen-MHC class II interaction*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了重组SpeA蛋白与人类MHC II类分子的复合物结构，揭示了其结合界面关键氨基酸残基，为开发阻断超抗原效应的抑制剂奠定理论基础。
3. **标题**: *Recombinant SpeA-based serodiagnosis of Streptococcus pyogenes infections*
**作者**: Wang Y, et al.
**摘要**: 开发基于重组SpeA的ELISA检测方法，用于快速诊断化脓性链球菌感染。临床样本验证显示高敏感性和特异性，表明其在流行病学监测中的潜在应用价值。
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建议通过PubMed或Google Scholar以关键词“recombinant SpeA”、“Streptococcus pyogenes exotoxin”检索最新文献获取准确信息。
**Background of SpeA Recombinant Protein**
Streptococcal pyrogenic exotoxin A (SpeA) is a superantigenic toxin produced by *Streptococcus pyogenes*, a Gram-positive bacterial pathogen responsible for infections ranging from mild pharyngitis to severe invasive diseases like necrotizing fasciitis and streptococcal toxic shock syndrome (STSS). SpeA, first identified in the 1920s, gained prominence due to its association with scarlet fever and toxin-mediated streptococcal outbreaks. It belongs to a family of exotoxins that disrupt immune regulation by binding simultaneously to major histocompatibility complex class II (MHC II) molecules on antigen-presenting cells and T-cell receptors (TCRs), triggering massive cytokine release. This hyperactivation contributes to systemic inflammation, tissue damage, and organ failure.
Recombinant SpeA (rSpeA) is engineered through cloning and expressing the *speA* gene in heterologous systems like *E. coli*. This approach ensures high purity and scalability, bypassing risks associated with native toxin purification. rSpeA retains the superantigenic properties of wild-type SpeA, making it a valuable tool for studying toxin-mediated pathogenesis, host immune responses, and therapeutic interventions. It is widely used in *in vitro* and *in vivo* models to investigate mechanisms of immune dysregulation and test neutralizing agents, including antibodies and vaccines.
Clinically, rSpeA aids in diagnosing past exposures via serological assays and informs vaccine design targeting conserved epitopes. Recent research also explores its role in autoimmune sequelae, such as rheumatic fever, linked to molecular mimicry. Despite advances, challenges remain in understanding strain-specific variations and optimizing therapeutic strategies. The development of rSpeA continues to drive innovations in combating streptococcal diseases and understanding superantigen biology.
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