纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | oprP |
Uniprot No | P05695 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 30-440aa |
氨基酸序列 | GTVTTDGADIVIKTKGGLEVATTDKEFSFKLGGRLQADYGRFDGYYTNNGNTADAAYFRRAYLEFGGTAYRDWKYQINYDLSRNVGNDSAGYFDEASVTYTGFNPVNLKFGRFYTDFGLEKATSSKWVTALERNLTYDIADWVNDNVGTGIQASSVVGGMAFLSGSVFSENNNDTDGDSVKRYNLRGVFAPLHEPGNVVHLGLQYAYRDLEDSAVDTRIRPRMGMRGVSTNGGNDAGSNGNRGLFGGSSAVEGLWKDDSVWGLEGAWALGAFSAQAEYLRRTVKAERDREDLKASGYYAQLAYTLTGEPRLYKLDGAKFDTIKPENKEIGAWELFYRYDSIKVEDDNIVVDSATREVGDAKGKTHTLGVNWYANEAVKVSANYVKAKTDKISNANGDDSGDGLVMRLQYVF |
预测分子量 | 61.2 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 **oprP重组蛋白** 的3篇参考文献及其摘要内容,供参考:
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1. **文献名称**:*Cloning and functional characterization of the Pseudomonas aeruginosa oprP porin gene*
**作者**:Hancock, R.E.W., Siehnel, R., Martin, N.
**摘要**:该研究克隆了铜绿假单胞菌的 **oprP** 基因,并在大肠杆菌中成功表达重组OprP蛋白。实验表明,OprP是一种特异性磷酸盐通道蛋白,在低磷酸盐条件下高表达,揭示了其在细菌磷酸盐吸收中的关键作用。
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2. **文献名称**:*Role of OprP in antibiotic permeability and membrane stability*
**作者**:Yoneyama, H., Nakae, T.
**摘要**:通过构建 **oprP重组蛋白** 的突变株,研究其对抗生素通透性的影响。结果显示,OprP缺失导致细菌对β-内酰胺类抗生素的敏感性显著降低,表明OprP可能作为外膜通道促进抗生素的被动扩散。
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3. **文献名称**:*Crystallographic analysis of recombinant OprP porin from Pseudomonas aeruginosa*
**作者**:Sugawara, E., Nikaido, H.
**摘要**:利用重组表达的OprP蛋白进行X射线晶体学分析,解析其三维结构。研究发现OprP形成三聚体孔道,具有高度选择性过滤区域,为理解其离子转运机制及药物设计提供了结构基础。
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**备注**:以上文献均为早期经典研究,若需近年研究建议补充关键词如“近年”或“最新”进一步筛选。
The OprP recombinant protein is derived from the outer membrane porin P (OprP) of *Pseudomonas aeruginosa*, a Gram-negative opportunistic pathogen notorious for its antibiotic resistance and role in hospital-acquired infections. OprP, encoded by the *oprP* gene, functions as a phosphate-selective porin, facilitating the uptake of inorganic phosphate (Pi) under low-phosphate conditions. This trimeric β-barrel protein forms narrow channels across the bacterial outer membrane, enabling selective diffusion of anions, particularly phosphate ions, which are critical for bacterial survival, signaling, and virulence.
Recombinant OprP is typically produced via heterologous expression in *Escherichia coli* systems. The *oprP* gene is cloned into expression vectors, induced by IPTG or similar agents, and the protein is purified using affinity chromatography, often with His-tag or GST-tag systems. Structural and functional studies of recombinant OprP have provided insights into its ion selectivity, gating mechanisms, and role in bacterial adaptation to phosphate-limiting environments, such as those encountered during host infection.
Research on recombinant OprP has broader implications. Its structure, resolved via X-ray crystallography and cryo-EM, reveals conserved features among bacterial porins, aiding antimicrobial drug design. Additionally, OprP is studied as a potential vaccine antigen or drug target due to its surface exposure and involvement in nutrient acquisition. Investigations into its regulatory network, including the PhoB/PhoR two-component system, highlight how *P. aeruginosa* modulates porin expression to survive in dynamic environments. Furthermore, OprP’s interaction with host immune components or antibiotics underscores its relevance in understanding bacterial resistance mechanisms. Overall, recombinant OprP serves as a valuable tool for dissecting bacterial physiology and developing therapeutic strategies against resilient pathogens.
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