| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | modA |
| Uniprot No | P37329 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-257aa |
| 氨基酸序列 | DEGKITVFAAASLTNAMQDIATQFKKEKGVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKAIDTATRQTLLGNSLVVVAPKASVQKDFTIDSKTNWTSLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLSPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPVAVVEGHNNATVKAFYDYLKGPQAAEIFKRYGFTIK |
| 预测分子量 | 37.9 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“ModA重组蛋白”的假设性参考文献示例(仅供参考，实际文献需通过学术数据库检索确认)：
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1. **文献名称**: *"High-yield expression and purification of recombinant ModA protein in E. coli for structural studies"*
**作者**: Smith, J. et al.
**摘要**: 研究利用大肠杆菌表达系统高效生产ModA重组蛋白，优化了诱导条件和纯化步骤，并通过质谱和圆二色光谱验证其正确折叠，为后续结构解析奠定基础。
2. **文献名称**: *"Crystal structure of ModA reveals a novel metal-binding mechanism in bacterial iron acquisition"*
**作者**: Tanaka, K. et al.
**摘要**: 通过X射线晶体学解析ModA的三维结构，揭示其与铁离子结合的特异性结构域，阐明其在细菌铁摄取中的关键作用及潜在抗菌靶点价值。
3. **文献名称**: *"Functional characterization of recombinant ModA in biofilm formation and antibiotic resistance"*
**作者**: Chen, L. et al.
**摘要**: 利用重组ModA蛋白进行功能实验，证明其通过调控细菌生物膜形成和膜通透性，影响病原菌对抗生素的耐药性。
4. **文献名称**: *"ModA-based subunit vaccine induces protective immunity against pathogenic strains in a murine model"*
**作者**: Gonzalez, M. et al.
**摘要**: 评估重组ModA作为亚单位疫苗的免疫原性，结果显示其能诱导小鼠产生特异性抗体并显著降低病原体载量，提示其疫苗开发潜力。
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**备注**：以上文献为示例，实际研究中请通过PubMed、Web of Science等平台以“ModA recombinant protein”或结合具体物种(如“Neisseria ModA”)为关键词检索最新文献。若“ModA”指代特定蛋白(如转运蛋白或毒力因子)，建议补充完整名称以提高检索准确性。
ModA recombinant protein is a engineered version of the ModA protein, originally identified in pathogenic *Neisseria* species as a crucial component of metal acquisition systems. This transmembrane protein functions as a substrate-binding subunit in ABC (ATP-binding cassette) transporters, primarily responsible for scavenging essential metals like iron and zinc from host environments. Its ability to bind multiple metal ions with high affinity makes it vital for bacterial survival during infection, particularly in iron-limited host conditions where pathogens compete with host proteins for metal nutrients.
The recombinant ModA protein is typically produced through heterologous expression in *E. coli* systems, enabling large-scale purification while retaining native metal-binding properties. Structural studies reveal conserved metal-binding motifs and a bilobed "Venus flytrap" domain that undergoes conformational changes during substrate uptake. Researchers often focus on its metal-binding extracellular loops, which show strain-specific variations potentially linked to host adaptation.
Current applications span multiple fields: In vaccinology, ModA serves as a vaccine candidate due to its surface exposure and role in virulence. Diagnostic developers exploit its metal-specific binding for biosensor designs. Biotechnology industries utilize engineered variants for metal recovery or purification processes. Additionally, it has become a model protein for studying metal homeostasis mechanisms and antimicrobial strategies targeting pathogen nutrient uptake.
Ongoing research investigates ModA's interactions with human metal-chelating proteins (e.g., transferrin) to develop metal-blocking therapies. Its recombinant form accelerates structural biology studies using X-ray crystallography and cryo-EM, while site-directed mutagenesis helps map functional domains. Recent preclinical studies explore ModA-based vaccines against antibiotic-resistant *Neisseria* strains, demonstrating cross-reactive immune responses in animal models.
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