| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ibpA |
| Uniprot No | P0C054 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-137aa |
| 氨基酸序列 | MRNFDLSPLY RSAIGFDRLF NHLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYID LERVIPEAKK PRRIEIN |
| 预测分子量 | 15,7 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 **ibpA重组蛋白** 的3篇参考文献概览：
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1. **文献名称**: *"IbpA and IbpB, the small heat shock proteins of Escherichia coli, function in the stabilization of aggregated proteins"*
**作者**: Kitagawa, M., et al.
**摘要**: 研究了大肠杆菌中小热休克蛋白IbpA和IbpB的功能，发现它们通过结合变性蛋白聚集体，在热应激条件下防止蛋白错误折叠，并协助伴侣蛋白系统(如ClpB/DnaK)进行后续修复。
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2. **文献名称**: *"The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state"*
**作者**: Matuszewska, M., et al.
**摘要**: 阐明了IbpA与IbpB协同作用机制，证明两者共同结合热诱导的蛋白聚集体，维持其处于可解聚状态，为后续ClpB和DnaK系统的高效修复提供基础。
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3. **文献名称**: *"Role of the Escherichia coli IbpA heat shock protein in the disaggregation of inclusion bodies"*
**作者**: Thomas, J.G., Baneyx, F.
**摘要**: 探讨了IbpA在重组蛋白包涵体解聚中的作用，表明过表达IbpA能增强包涵体溶解效率，并提升重组蛋白的活性回收率，为优化重组蛋白生产提供策略。
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以上文献均聚焦于IbpA在蛋白质量控制、应激响应及重组蛋白生产中的应用机制。如需具体文献链接或补充，可进一步提供数据库检索关键词(如DOI或PMID)。
The IbpA (Iron-regulated Bordetella pertussis autotransporter) recombinant protein is derived from the pathogenic bacterium *Bordetella pertussis*, the causative agent of whooping cough. Autotransporter proteins, a class of virulence factors in Gram-negative bacteria, are characterized by their ability to self-transport across the bacterial outer membrane. IbpA is notably expressed under iron-limiting conditions, a common stress encountered during host infection, suggesting its role in iron acquisition or immune evasion. The protein features a conserved C-terminal β-barrel domain that facilitates autotransport and an N-terminal passenger domain responsible for host-pathogen interactions.
Recombinant IbpA is engineered for heterologous expression, typically in *E. coli*, to study its structural and functional properties without handling the pathogen itself. Its iron-regulated expression hints at involvement in bacterial survival mechanisms, potentially aiding adhesion to host cells or countering iron-sequestering host defenses like lactoferrin. Studies also suggest IbpA may contribute to biofilm formation, enhancing bacterial persistence in the respiratory tract.
Research on IbpA recombinant protein focuses on its application in vaccine development, as it elicits immune responses in animal models. Its immunogenicity and surface exposure make it a candidate for subunit vaccines or diagnostic tools. Additionally, studying IbpA’s interactions with host cells provides insights into *B. pertussis* pathogenesis and potential therapeutic targets. Recombinant technology enables scalable production, high purity, and site-specific modifications for functional studies, accelerating both basic research and translational applications.
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