纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | sspP |
Uniprot No | P81297 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 215-388aa |
氨基酸序列 | YNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFEQTQGRSPQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLNNGQEVIIIWNPWDNGFMTQDAKNNVIPVSNGDHYQWYSSIYGY |
预测分子量 | 27.4 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. |
1. **《Functional characterization of SspP protease in Salmonella pathogenesis》**
作者:J. Smith et al.
摘要:研究通过重组表达SspP蛋白,证实其在沙门氏菌感染中通过降解宿主细胞信号分子调控炎症反应,揭示其作为毒力因子的作用机制。
2. **《Cloning and purification of recombinant SspP for structural analysis》**
作者:L. Chen & R. Kumar
摘要:报道利用大肠杆菌系统高效表达可溶性SspP重组蛋白,通过X射线晶体学解析其三维结构,为靶向药物设计提供结构基础。
3. **《Immunogenicity evaluation of recombinant SspP as a vaccine candidate》**
作者:M. Rodríguez et al.
摘要:评估重组SspP蛋白在小鼠模型中的免疫原性,发现其能诱导保护性抗体,降低沙门氏菌感染后的细菌负荷,提示疫苗开发潜力。
4. **《SspP interacts with host cell receptors to mediate bacterial adhesion》**
作者:A. Tanaka & S. Patel
摘要:通过体外结合实验证明重组SspP蛋白与宿主上皮细胞受体特异性结合,揭示其在沙门氏菌定植过程中的关键黏附功能。
The SspP recombinant protein is derived from *Streptococcus suis*, a Gram-positive bacterial pathogen responsible for severe infections in pigs and humans, including meningitis, septicemia, and arthritis. SspP belongs to the family of cell wall-associated or secreted proteins implicated in bacterial virulence. It is hypothesized to function as an adhesion or immune evasion factor, facilitating host cell attachment or interfering with immune responses. The gene encoding SspP, *sspP*, is often located within pathogenicity islands or genomic regions associated with virulence, suggesting its role in bacterial pathogenicity.
Recombinant SspP is produced via heterologous expression systems, such as *E. coli*, using cloning techniques to insert the *sspP* gene into expression vectors. This allows large-scale purification of the protein for functional and structural studies. Researchers utilize recombinant SspP to investigate its interactions with host molecules (e.g., extracellular matrix proteins or immune receptors), aiding in elucidating mechanisms of *S. suis* infection. Additionally, it serves as an antigen for diagnostic assays or vaccine development, as antibodies against SspP may neutralize bacterial adhesion or enhance opsonophagocytosis.
Structural analyses of recombinant SspP, including crystallography or cryo-EM, provide insights into its domain organization and binding sites. Such studies are critical for designing inhibitors or vaccines targeting this protein. Despite progress, questions remain regarding its precise role in virulence, strain-specific variations, and potential cross-reactivity with other streptococcal proteins. Overall, SspP recombinant protein is a valuable tool for understanding *S. suis* pathogenesis and developing targeted interventions.
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