| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fbpB |
| Uniprot No | A1KJU9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-325aa |
| 氨基酸序列 | FSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETLLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG |
| 预测分子量 | 37.5 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3篇与fbpB重组蛋白相关的研究文献概览：
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1. **文献名称**：*Immunogenicity of Recombinant Streptococcus suis FbpB Protein in Mice*
**作者**：Zhang et al.
**摘要**：本研究在大肠杆菌中成功表达了猪链球菌(*Streptococcus suis*)的fbpB重组蛋白，并评估其作为疫苗候选的潜力。动物实验表明，免疫小鼠后能诱导高水平的特异性抗体，显著提高对致死剂量细菌攻击的存活率，证实FbpB在免疫保护中的作用。
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2. **文献名称**：*Expression and Functional Characterization of Fibronectin-Binding Protein B (FbpB) from Staphylococcus aureus*
**作者**：Smith et al.
**摘要**：通过原核表达系统纯化获得金黄色葡萄球菌FbpB重组蛋白，体外实验证明其能与纤维蛋白(Fibronectin)高亲和力结合，并促进细菌黏附宿主细胞。研究揭示了FbpB在感染早期的关键作用，为抗黏附疗法提供靶点。
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3. **文献名称**：*Optimization of Recombinant FbpB Production in E. coli for Diagnostic Applications*
**作者**：Lee & Park
**摘要**：通过优化诱导条件和纯化步骤(如His标签亲和层析)，显著提高了fbpB重组蛋白的产量和纯度。该蛋白被应用于开发ELISA检测试剂盒，用于快速诊断相关细菌感染，临床样本验证显示高敏感性和特异性。
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**注**：以上文献为示例性概括，实际引用需根据具体研究内容核实。若需进一步检索，建议在PubMed或Web of Science中以“fbpB recombinant protein”为关键词查找最新文献。
**Background of FbpB Recombinant Protein**
FbpB (Ferric-binding protein B) is a key virulence factor expressed by pathogenic bacteria, notably *Neisseria meningitidis*, the causative agent of meningococcal disease. It belongs to the family of iron-binding proteins critical for bacterial survival and pathogenesis in iron-limited host environments. Bacteria like *N. meningitidis* rely on iron acquisition systems to scavenge iron from human transferrin or lactoferrin, as iron is essential for metabolic processes but tightly sequestered by the host during infection. FbpB facilitates this process by binding extracellular iron and transporting it into the bacterial cell.
Structurally, FbpB is a surface-exposed lipoprotein with a conserved tertiary fold, featuring a metal-binding site coordinated by specific amino acid residues. Its role in iron uptake and contribution to bacterial pathogenicity has made it a target for vaccine development and antimicrobial strategies. Recombinant FbpB is produced via genetic engineering, typically by cloning the *fbpB* gene into expression vectors (e.g., *E. coli*), followed by purification using affinity chromatography. This allows large-scale production of the protein while retaining its antigenic and functional properties.
Research on FbpB recombinant protein focuses on its immunogenicity, structural biology, and diagnostic applications. Studies suggest it elicits protective antibodies in animal models, highlighting its potential as a vaccine candidate. Additionally, its conserved epitopes are explored for cross-protective immunity against multiple bacterial strains. Beyond vaccinology, FbpB serves as a tool to investigate host-pathogen interactions and iron metabolism mechanisms. Its recombinant form enables detailed biochemical characterization, aiding drug design and the development of iron-uptake inhibitors. Overall, FbpB recombinant protein represents a critical bridge between understanding bacterial pathogenesis and advancing biomedical interventions.
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