纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | hlgC |
Uniprot No | Q7A3S2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 30-315aa |
氨基酸序列 | ANDTEDIGKGSDIEIIKRTEDKTSNKWGVTQNIQFDFVKDKKYNKDALILKMQGFISSRTTYYNYKKTNHVKAMRWPFQYNIGLKTNDKYVSLINYLPKNKIESTNVSQTLGYNIGGNFQSAPSLGGNGSFNYSKSISYTQQNYVSEVEQQNSKSVLWGVKANSFATESGQKSAFDSDLFVGYKPHSKDPRDYFVPDSELPPLVQSGFNPSFIATVSHEKGSSDTSEFEITYGRNMDVTHAIKRSTHYGNSYLDGHRVHNAFVNRNYTVKYEVNWKTHEIKVKGQN |
预测分子量 | 39.5 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hlgC重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**: "Purification and characterization of HlgC, a component of the Staphylococcus aureus gamma-hemolysin"
**作者**: Baba-Moussa, L., et al.
**摘要**: 该研究报道了重组HlgC蛋白在大肠杆菌中的表达与纯化,证实其与HlgB协同作用可诱导红细胞溶血,揭示了其在金黄色葡萄球菌毒力中的关键作用。
2. **文献名称**: "Structural and functional analysis of the pore-forming component HlgC from Staphylococcus aureus"
**作者**: Yamashita, K., et al.
**摘要**: 通过X射线晶体学解析了重组HlgC蛋白的三维结构,发现其与HlgB结合后形成跨膜孔道,阐明了其破坏宿主细胞膜的分子机制。
3. **文献名称**: "Recombinant HlgC as a potential vaccine candidate against Staphylococcus aureus infection"
**作者**: Chen, X., et al.
**摘要**: 评估了重组HlgC蛋白在小鼠模型中的免疫保护效果,表明其可诱导中和抗体并减少细菌载量,提示其作为葡萄球菌疫苗组分的潜力。
(注:上述文献为示例性概括,实际文献需通过学术数据库检索确认。)
**Background of HLgC Recombinant Protein**
HLgC (gamma-hemolysin component C) is a key virulence factor produced by *Staphylococcus aureus*, a Gram-positive pathogen associated with diverse infections ranging from skin abscesses to life-threatening conditions like sepsis and pneumonia. Gamma-hemolysin is a two-component pore-forming toxin composed of two subunits, HlgA/HlgB and HlgC/HlgB, with HlgC pairing specifically with HlgB to form the functional toxin. This bipartite toxin targets host cell membranes, disrupting cellular integrity and contributing to immune evasion and tissue damage during infection.
Structurally, HlgC belongs to the β-barrel pore-forming toxin family. It is secreted as a water-soluble monomer that binds to host cell receptors, such as complement component C5a receptor 1 (C5aR1) or CXCR2. enabling oligomerization with HlgB on the membrane surface. This assembly triggers pore formation, leading to ion imbalance, osmotic lysis, and cell death. HlgC’s role in pathogenicity is further linked to its ability to lyse erythrocytes, neutrophils, and endothelial cells, facilitating bacterial spread and immune suppression.
Recombinant HlgC protein is generated via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional and structural studies. Its production enables research into toxin-receptor interactions, mechanisms of membrane perforation, and potential therapeutic strategies. For instance, neutralizing antibodies or inhibitors targeting HlgC could mitigate *S. aureus* virulence. Additionally, recombinant HlgC serves as an antigen in vaccine development and diagnostic tools, given its specificity and role in severe infections.
The rise of antibiotic-resistant *S. aureus* strains, including MRSA, underscores the urgency to explore alternative treatments. Studying HlgC’s molecular pathways not only enhances understanding of staphylococcal pathogenesis but also identifies novel targets for anti-virulence therapies, offering a promising avenue to combat this resilient pathogen.
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