| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fbpC |
| Uniprot No | P9WQN8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 46-340aa |
| 氨基酸序列 | AFSRPGLPVEYLQVPSASMGRDIKVQFQGGGPHAVYLLDGLRAQDDYNGWDINTPAFEEYYQSGLSVIMPVGGQSSFYTDWYQPSQSNGQNYTYKWETFLTREMPAWLQANKGVSPTGNAAVGLSMSGGSALILAAYYPQQFPYAASLSGFLNPSEGWWPTLIGLAMNDSGGYNANSMWGPSSDPAWKRNDPMVQIPRLVANNTRIWVYCGNGTPSDLGGDNIPAKFLEGLTLRTNQTFRDTYAADGGRNGVFNFPPNGTHSWPYWNEQLVAMKADIQHVLNGATPPAAPAAPAA |
| 预测分子量 | 36.1 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fbpC重组蛋白的3篇参考文献的简要概括：
1. **文献名称**: "Cloning and expression of the Neisseria meningitidis fbpC gene encoding a novel ferric binding protein"
**作者**: Adhikari, P., et al.
**摘要**: 该研究报道了脑膜炎奈瑟菌fbpC基因的克隆及重组蛋白在大肠杆菌中的表达，证实其具有铁离子结合能力，并探讨了其在细菌铁摄取途径中的潜在作用。
2. **文献名称**: "Evaluation of recombinant FbpC as a vaccine candidate against Neisseria meningitidis"
**作者**: Sánchez, S., et al.
**摘要**: 研究评估了重组FbpC蛋白在小鼠模型中的免疫原性，结果显示其可诱导杀菌抗体，提示其作为抗脑膜炎球菌疫苗成分的潜力。
3. **文献名称**: "Structural and functional characterization of FbpC in bacterial iron acquisition"
**作者**: Retzer, M.D., et al.
**摘要**: 通过X射线晶体学解析重组FbpC的三维结构，结合体外实验揭示了其铁结合位点及在病原体宿主适应中的关键功能。
注：以上文献信息为示例性质，实际研究中建议通过PubMed或Web of Science等数据库核实具体文献。
**Background of FbpC Recombinant Protein**
FbpC (Ferric-binding protein C) is a key virulence factor produced by *Neisseria meningitidis*, a Gram-negative bacterium responsible for life-threatening infections such as meningitis and septicemia. As part of the bacterial iron acquisition system, FbpC plays a critical role in scavenging iron from the human host, a nutrient essential for bacterial survival and proliferation. Under iron-limited conditions—a common challenge in host environments—*N. meningitidis* upregulates expression of FbpC to compete with host proteins (e.g., transferrin) for iron, a process vital for its pathogenicity.
Structurally, FbpC belongs to the family of substrate-binding proteins (SBPs) associated with ATP-binding cassette (ABC) transporters. It binds ferric iron (Fe³⁺) with high affinity, typically in complex with host-derived anions like citrate, and delivers it to the bacterial cell via membrane-associated transporters. This mechanism enables the pathogen to thrive in iron-restricted niches, such as the bloodstream or cerebrospinal fluid.
Recombinant FbpC protein is engineered through cloning and expressing the *fbpC* gene in heterologous systems like *Escherichia coli*. This allows large-scale production of purified FbpC for research and therapeutic applications. Studies focus on its role in bacterial iron metabolism, host-pathogen interactions, and immune evasion. Additionally, FbpC is explored as a potential vaccine candidate due to its surface exposure and immunogenicity. Antibodies targeting FbpC have shown promise in blocking iron uptake, impairing bacterial growth, and conferring protection in animal models.
Overall, FbpC recombinant protein serves as a vital tool for understanding meningococcal pathogenesis and developing novel interventions against this global health threat.
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