| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fbpA |
| Uniprot No | P02730 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-911aa |
| 氨基酸序列 | MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV |
| 预测分子量 | 101,7 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fbpA重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *"Cloning, expression, and purification of the Mycobacterium tuberculosis fbpA gene encoding a novel immunogenic protein"*
**作者**: Horwitz MA, et al.
**摘要**: 该研究报道了结核分枝杆菌fbpA基因的克隆及在大肠杆菌中的重组表达。纯化的FbpA蛋白在动物模型中显示出强烈的免疫原性，提示其作为结核病亚单位疫苗的潜在应用价值。
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2. **文献名称**: *"Functional characterization of the iron-binding protein FbpA in Neisseria meningitidis"*
**作者**: Retzer MD, et al.
**摘要**: 文章通过重组表达脑膜炎奈瑟菌FbpA蛋白，分析了其铁离子结合能力及在细菌铁摄取中的作用。实验表明FbpA通过特异性与铁结合并转运至细菌内，为开发靶向铁代谢的抗菌策略提供依据。
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3. **文献名称**: *"Recombinant FbpA-based ELISA for serodiagnosis of tuberculosis"*
**作者**: Laal S, et al.
**摘要**: 研究利用重组FbpA蛋白建立了一种新型ELISA检测方法，用于结核病血清学诊断。临床样本验证显示，该方法具有高灵敏度和特异性，可作为结核病快速诊断工具。
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注：上述文献信息为示例，实际引用时建议通过PubMed或Web of Science核对原文准确性。
**Background of FbpA Recombinant Protein**
FbpA (Ferric-binding protein A) is a periplasmic iron-binding protein primarily studied in pathogenic bacteria, notably *Neisseria meningitidis* and other Gram-negative species. It plays a critical role in iron acquisition, a process vital for bacterial survival and virulence, as iron is essential for metabolic processes but often limited in host environments. FbpA binds ferric ions (Fe³⁺) with high affinity via a conserved metal-binding site, typically involving a triad of amino acid residues (e.g., His, Tyr, Glu), and facilitates iron transport across the bacterial membrane through interactions with specific ABC transporters.
The recombinant FbpA protein is engineered via cloning and expressing the *fbpA* gene in heterologous systems like *E. coli* or yeast. This allows large-scale production of purified, soluble FbpA for structural, functional, and immunological studies. Its recombinant form retains the native protein’s metal-binding capacity and structural integrity, making it a valuable tool for studying bacterial iron homeostasis, host-pathogen interactions, and potential therapeutic targets.
In vaccine research, FbpA has been explored as a candidate antigen due to its surface exposure and conservation across strains. Preclinical studies highlight its ability to elicit protective antibodies in animal models, though clinical validation remains ongoing. Additionally, recombinant FbpA is used in diagnostic assays to detect pathogen-specific immune responses.
Recent advances in structural biology, such as X-ray crystallography, have resolved FbpA’s metal-bound conformations, providing insights into its dynamic binding mechanisms. These studies underscore its dual role as a virulence factor and a model for understanding microbial nutrient scavenging. Overall, FbpA recombinant protein serves as a multifaceted resource in microbiology, immunology, and antimicrobial development.
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