| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | sip |
| Uniprot No | Q9EU98 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-434aa |
| 氨基酸序列 | QETDTTWTARTVSEVKADLVKQDNKSSYTVKYGDTLSVISEAMSIDMNVLAKINNIADINLIYPETTLTVTYDQKSHTATSMKIETPATNAAGQTTATVDLKTNQVFVADQKVSLNTISEGMTPEAATTIVSPMKTYSSAPALKSKEVLAQEQAVSQVAANEQVSPAPVKSITSEVPAAKEEVKPTQTSVSQLTTVSPASVAAETPAPVAKVAPVRTVAAPRVASAKVVTPKVETGASPEHVSAPAVPVTTTSPATDSKLQATEVKSVPVAQKAPTATPVAQPASTTNAVAAHPENAGLQPHVAAYKEKVASTYGVNEFSTYRAGDPGDHGKGLAVDFIVGKNQALGNEVAQYSTQNMAANNISYVIWQQKFYSNTNSIYGPANTWNAMPDRGGVTANHYDHVHVSFNK |
| 预测分子量 | 50.5 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SIP重组蛋白的3篇参考文献示例(注：文献为虚拟示例，实际引用需核实真实来源)：
1. **文献名称**：*Structural and functional characterization of streptococcal SIP protein in immune modulation*
**作者**：Smith J, et al.
**摘要**：研究通过重组技术表达链球菌SIP蛋白，解析其晶体结构，证明其通过结合宿主免疫细胞表面受体抑制炎症反应，为免疫调节机制提供新见解。
2. **文献名称**：*Recombinant SIP protein as a novel vaccine adjuvant: Enhanced antibody response in murine models*
**作者**：Wang L, et al.
**摘要**：利用重组SIP蛋白作为疫苗佐剂，在小鼠模型中显著增强抗原特异性抗体滴度，并激活TLR2通路，提示其在疫苗开发中的潜在应用价值。
3. **文献名称**：*Antiviral activity of SIP against influenza A virus via blocking viral entry*
**作者**：Kim S, et al.
**摘要**：发现重组SIP蛋白可通过竞争性结合宿主细胞表面受体(如HA蛋白结合位点)，抑制流感病毒入侵，为抗病毒药物研发提供新策略。
(若需实际文献，建议在PubMed/Google Scholar检索关键词：recombinant SIP protein, streptococcal inhibitor of complement, immune modulation)
**Background of SIP Recombinant Proteins**
SIP (Surface Immunogenic Protein) recombinant proteins are engineered molecules derived from pathogenic organisms, primarily bacteria, and produced via recombinant DNA technology. These proteins are designed to mimic specific antigenic components of pathogens, enabling their use in vaccine development and immunological research. SIPs are often identified as virulence factors or surface-exposed antigens critical for pathogen adhesion, invasion, or immune evasion. By isolating and expressing the genes encoding these proteins in heterologous host systems (e.g., *E. coli*, yeast, or mammalian cells), researchers can produce purified SIPs for targeted applications.
The development of SIP recombinant proteins is driven by the need for safer and more effective vaccines. Traditional whole-pathogen vaccines carry risks of incomplete attenuation or adverse immune reactions. In contrast, subunit vaccines based on recombinant SIPs focus immune responses on key protective antigens, reducing side effects while enhancing specificity. For example, SIPs from *Streptococcus* species (e.g., Group B *Streptococcus*) have been explored as vaccine candidates due to their role in bacterial colonization and immune system interaction.
Advances in bioinformatics and structural biology have accelerated SIP identification and optimization. Epitope mapping and protein engineering techniques improve antigen stability, solubility, and immunogenicity. Challenges remain, including ensuring proper protein folding post-expression and maintaining conformational epitopes critical for neutralizing antibody responses.
SIP recombinant proteins also serve as tools for diagnostic assays and therapeutic antibody production. Their versatility and scalability make them pivotal in combating infectious diseases, particularly antibiotic-resistant pathogens. Ongoing research aims to expand their applications to cancer immunotherapy and personalized medicine, leveraging their ability to elicit targeted immune responses.
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