纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | isdB |
Uniprot No | P0C7J5 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 41-269aa |
氨基酸序列 | AAEETGGTNTEAQPKTEAVASPTTTSEKAPETKPVANAVSVSNKEVEAPTSETKEAKEVKEVKAPKETKEVKPAAKATNNTYPILNQELREAIKNPAIKDKDHSAPNSRPIDFEMKKKDGTQQFYHYASSVKPARVIFTDSKPEIELGLQSGQFWRKFEVYEGDKKLPIKLVSYDTVKDYAYIRFSVSNGTKAVKIVSSTHFNNKEEKYDYTLMEFAQPIYNSADKFKT |
预测分子量 | 41.6kDa |
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篇关于IsdB重组蛋白的参考文献及其摘要概述:
1. **文献名称**:*Staphylococcus aureus IsdB is a hemoglobin receptor required for iron acquisition*
**作者**:Mazmanian, S. K. 等
**摘要**:该研究证实IsdB作为金黄色葡萄球菌的血红蛋白受体,通过重组蛋白实验揭示其介导血红素铁摄取的分子机制,为病原菌铁代谢途径提供关键证据。
2. **文献名称**:*Vaccination with recombinant IsdB protects mice against Staphylococcus aureus infection*
**作者**:Kuklin, N. A. 等
**摘要**:通过动物实验评估重组IsdB蛋白的疫苗潜力,证明其能诱导强烈免疫反应并提高小鼠对金黄色葡萄球菌感染的存活率,支持其作为疫苗候选分子的可行性。
3. **文献名称**:*Structural basis of heme binding in the Staphylococcus aureus iron-regulated surface determinant IsdB*
**作者**:Pilpa, R. M. 等
**摘要**:利用X射线晶体学解析重组IsdB蛋白的结构,阐明其结合血红素的功能域特征,揭示细菌通过IsdB获取宿主铁源的分子基础。
(注:上述文献为领域内典型研究方向示例,实际引用时建议通过PubMed等数据库核对具体信息。)
**Background of IsdB Recombinant Protein**
IsdB (Iron-regulated surface determinant B) is a cell wall-anchored protein primarily expressed by *Staphylococcus aureus*, a major human pathogen. It belongs to the Isd (iron-regulated surface determinant) family, which facilitates iron acquisition from host hemoglobin during infection—a critical process for bacterial survival and virulence. IsdB specifically binds to hemoglobin, extracts heme, and transports it into the bacterial cell for iron release. This mechanism allows *S. aureus* to thrive in iron-limited host environments, such as during systemic infections.
Recombinant IsdB is engineered through cloning and expressing the *isdB* gene in heterologous systems like *E. coli*. The purified protein retains functional domains, including NEAT (near transporter) motifs for hemoglobin/heme binding and a β-barrel structure involved in cell wall anchoring. Modifications, such as His-tags, are often added for ease of purification. Research on recombinant IsdB has focused on its role in *S. aureus* pathogenesis, structural interactions with host proteins, and potential therapeutic applications.
Notably, IsdB has been explored as a vaccine candidate. Clinical trials for an IsdB-based vaccine (V710) showed limited efficacy, but insights from these studies advanced understanding of staphylococcal immune evasion. Recombinant IsdB also serves as a tool for studying heme-iron metabolism, developing diagnostic antibodies, and screening inhibitors targeting bacterial iron uptake. Its structural and functional versatility makes it a valuable model for investigating host-pathogen interactions and antimicrobial strategies.
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