| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | cap8A |
| Uniprot No | O15479 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-319aa |
| 氨基酸序列 | MESTLELTKIKEVLQKNLKILIILPLLFLIISAIVTFFVLSPKYQANTQILVNQTKGDNPQFMAQEVQSNIQLVNTYKEIVKSPRILDEVSKDLNNKYSPSKLSSMLTITNQENTQLINIQVKSGHKQDSEKIANSFAKVTSKQIPKIMSLDNVSILSKADGTAVKVAPKTVVNLIGAFFLGLVVALIYIFFKVIFDKRIKDEEDVEKELGLPVLGSIQKFN |
| 预测分子量 | 26.4 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. |
以下是3篇关于cap8A重组蛋白的参考文献摘要整理(文献标题与作者为虚构示例，供格式参考)：
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1. **文献名称**: *Molecular characterization of the cap8A gene in Staphylococcus aureus capsule biosynthesis*
**作者**: Lee, J. et al. (2015)
**摘要**: 研究通过克隆cap8A基因并在大肠杆菌中表达重组蛋白，证明Cap8A蛋白在金黄色葡萄球菌8型荚膜多糖合成中具有糖基转移酶活性，揭示了其底物特异性及对细菌毒力的影响。
2. **文献名称**: *Recombinant Cap8A as a vaccine candidate against S. aureus infections*
**作者**: Zhang, R. & Wang, H. (2018)
**摘要**: 通过纯化重组Cap8A蛋白并免疫小鼠，实验显示该蛋白能诱导高水平IgG抗体，显著降低金黄色葡萄球菌感染后的细菌载量，表明其在亚单位疫苗开发中的潜在价值。
3. **文献名称**: *Structural insights into Cap8A-mediated polysaccharide polymerization*
**作者**: Müller, C. et al. (2020)
**摘要**: 利用X射线晶体学解析重组Cap8A蛋白的三维结构，发现其N端结构域负责识别底物UDP-糖分子，C端催化结构域驱动多糖链延伸，为靶向抑制剂设计提供依据。
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注：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science以关键词"cap8A recombinant protein"+"Staphylococcus aureus"检索真实文献。
**Background of Cap8A Recombinant Protein**
*Staphylococcus aureus* (S. aureus), a Gram-positive pathogen, is a leading cause of healthcare- and community-associated infections, ranging from skin abscesses to life-threatening conditions like sepsis. Its virulence is partly attributed to surface-associated virulence factors, including capsular polysaccharides (CPs), which protect the bacterium from host immune defenses. Among 11 known CP serotypes, CP5 and CP8 are predominant in clinical isolates, particularly in antibiotic-resistant strains like methicillin-resistant *S. aureus* (MRSA).
The *cap8* gene cluster encodes enzymes and regulatory proteins required for CP8 biosynthesis. Cap8A, a key protein within this operon, is hypothesized to function as a glycosyltransferase or polymerase, directly participating in CP8 assembly. CPs are immunologically relevant; antibodies targeting CPs enhance opsonophagocytic clearance of the pathogen. However, natural CPs are poorly immunogenic alone, necessitating conjugation to carrier proteins (e.g., CRM197) for vaccine development.
Recombinant Cap8A protein, produced via heterologous expression systems (e.g., *E. coli*), serves as a tool to study CP8 biosynthesis mechanisms and structure-function relationships. It also holds potential as a diagnostic antigen or vaccine component. Preclinical studies suggest that Cap8A-based vaccines may elicit protective immunity, though challenges remain in optimizing immunogenicity and overcoming strain-specific CP variability.
Current research focuses on combining CP antigens with other virulence factors (e.g., toxins) to develop broad-spectrum vaccines. Recombinant Cap8A, alongside other *cap* proteins, provides a platform to dissect CP8’s role in immune evasion and explore therapeutic strategies against CP8-expressing *S. aureus* strains, particularly in an era of rising antimicrobial resistance.
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