| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | MSA2 |
| Uniprot No | P50498 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 109-246aa |
| 氨基酸序列 | NDAEASTSTSSENPNHKNAETNPKGKGEVQEPNQANKETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNN |
| 预测分子量 | 16.7 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MSA2重组蛋白的假设参考文献示例(内容为虚构，仅用于演示格式)：
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1. **《Efficient expression and purification of recombinant MSA2 antigen in Escherichia coli》**
*Authors: Zhang L, Wang Y, Chen H (2020)*
*Journal: Protein Expression and Purification*
摘要：本研究报道了通过大肠杆菌表达系统高效生产疟原虫MSA2重组蛋白的优化方法，采用亲和层析纯化技术获得高纯度蛋白，验证其免疫原性适用于疫苗开发。
2. **《MSA2 as a diagnostic marker: Serological evaluation in autoimmune diseases》**
*Authors: Gupta S, et al. (2018)*
*Journal: Clinical Immunology*
摘要：通过重组MSA2蛋白建立ELISA检测方法，发现其在系统性硬化症患者血清中特异性抗体水平显著升高，提示MSA2可能作为新型自身免疫标志物。
3. **《Structural and functional analysis of MSA2 protein from Mycobacterium tuberculosis》**
*Authors: Kim J, et al. (2021)*
*Journal: Scientific Reports*
摘要：解析结核分枝杆菌MSA2蛋白的晶体结构，揭示其与宿主细胞互作的分子机制，为基于MSA2靶点的抗结核药物设计提供理论依据。
4. **《Recombinant MSA2-based vaccine confers protection against Schistosoma infection in mice》**
*Authors: Oliveira R, et al. (2019)*
*Journal: Vaccine*
摘要：利用重组MSA2蛋白联合佐剂免疫小鼠，诱导Th1型免疫反应并显著降低血吸虫感染负荷，证明其作为候选疫苗的潜力。
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注：以上文献为模拟内容，实际研究中请通过PubMed或Web of Science等数据库检索真实发表的论文。
**Background of MSA2 Recombinant Protein**
The MSA2 (Merozoite Surface Antigen 2) recombinant protein is a candidate antigen for malaria vaccine development, primarily targeting *Plasmodium falciparum*, the deadliest malaria-causing parasite. During the parasite’s blood-stage infection, merozoites invade red blood cells (RBCs), a process mediated by surface proteins like MSA2. This antigen is exposed on the merozoite surface and plays a role in RBC recognition and invasion, making it a promising target for antibodies to block infection.
MSA2 exhibits genetic polymorphism across parasite strains, complicating vaccine design. To address this, recombinant MSA2 proteins are engineered to include conserved epitopes critical for immune recognition. Advances in genetic engineering enable the production of stabilized, full-length or truncated MSA2 variants in heterologous systems (e.g., *E. coli* or yeast), ensuring proper folding and immunogenicity. These recombinant proteins often incorporate fusion partners or adjuvants to enhance stability and immune responses.
Preclinical studies show that MSA2-based vaccines elicit antibodies that inhibit merozoite invasion *in vitro* and reduce parasitemia in animal models. Some formulations combine MSA2 with other blood-stage antigens (e.g., MSP1. AMA1) or fusion constructs (e.g., GMZ2) to broaden protection. Clinical trials have evaluated safety and immunogenicity, with mixed results highlighting challenges like antigenic variability and suboptimal immune memory.
Current research focuses on optimizing MSA2 constructs, leveraging structural biology to identify conserved functional domains, and incorporating novel adjuvants or delivery platforms (e.g., viral vectors, nanoparticles). These efforts aim to overcome strain-specific immunity and enhance cross-protective efficacy, advancing MSA2 as a component of next-generation multi-antigen malaria vaccines.
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