| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ompK |
| Uniprot No | P59570 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-266aa |
| 氨基酸序列 | ADYSDGDIHKNDYKWMQFNLMGAFDELPGESSHDYLEMEFGGRSGIFDLYGYVDVFNLASDKGSDKVGDPKIFMKFAPRMSIDGLTGKDLSFGPVQELYVATLFEWDGTDYKTNPFSVNNQKVGIGSDVMVPWFGKVGVNLYGTYQGNQKDWNGFQISTNWFKPFYFFENGSFISYQGYIDYQFGMKEKYSSASNGGAMFNGIYWHSDRFAVGYGLKGYKDVYGIKDSDALKSTGFGHYVAVTYKF |
| 预测分子量 | 43.9 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ompK重组蛋白的模拟参考文献示例(仅供学术参考，具体文献需通过数据库核实)：
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1. **文献名称**：Cloning, Expression, and Purification of Recombinant OmpK from *Klebsiella pneumoniae*
**作者**：Zhang L. et al.
**摘要**：该研究成功克隆了肺炎克雷伯菌的ompK基因，并在大肠杆菌中实现高效表达，通过亲和层析纯化获得重组OmpK蛋白，验证其与抗生素渗透性相关的跨膜结构特征。
2. **文献名称**：Immunogenicity Evaluation of Recombinant OmpK as a Vaccine Candidate
**作者**：Wang Y. et al.
**摘要**：评估重组OmpK蛋白在小鼠模型中的免疫原性，证明其可诱导特异性抗体产生，并对肺炎克雷伯菌感染提供部分保护，提示其作为疫苗组分的潜力。
3. **文献名称**：Recombinant OmpK as a Diagnostic Antigen for Serological Detection
**作者**：Singh R. et al.
**摘要**：将重组OmpK蛋白用于ELISA检测，证实其对临床样本中肺炎克雷伯菌抗体的高敏感性和特异性，支持其在快速诊断中的应用。
4. **文献名称**：Structural Insights into OmpK Porin Function via Recombinant Protein Analysis
**作者**：Chen H. et al.
**摘要**：通过重组OmpK蛋白的晶体结构解析，揭示其β-桶状结构及与碳青霉烯类抗生素的相互作用机制，为耐药性研究提供分子基础。
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提示：实际文献需通过PubMed、Web of Science或Google Scholar等平台，以关键词“recombinant OmpK”或“OmpK cloning”检索。
**Background of OmpK Recombinant Protein**
OmpK (outer membrane protein K) is a porin protein primarily found in the outer membrane of Gram-negative bacteria, notably within the *Enterobacteriaceae* family, such as *Klebsiella pneumoniae*. Porins like OmpK form β-barrel channels that regulate the passive diffusion of small molecules, including nutrients and antimicrobial agents, across the bacterial membrane. In pathogenic strains, OmpK plays a critical role in antibiotic resistance by modulating membrane permeability. For instance, reduced expression or mutations in OmpK can limit the influx of β-lactams, carbapenems, and other antibiotics, contributing to multidrug-resistant phenotypes.
Recombinant OmpK refers to the protein produced via genetic engineering, typically by cloning the *ompK* gene into expression vectors (e.g., *E. coli*) followed by purification. This approach enables large-scale production of the protein for functional and structural studies. Researchers utilize recombinant OmpK to investigate its role in bacterial virulence, antibiotic uptake, and immune evasion. Its structural features, such as extracellular loops and channel properties, are analyzed to understand interactions with host immune components or antimicrobial compounds.
In biomedical applications, recombinant OmpK serves as a potential diagnostic antigen or vaccine candidate. For example, antibodies against OmpK can detect *K. pneumoniae* infections in clinical samples. Additionally, OmpK-based vaccines aim to elicit protective immunity by targeting surface-exposed epitopes. Studies also explore its utility in designing inhibitors to block porin-mediated antibiotic resistance. However, challenges remain, including antigenic variability among OmpK subtypes (e.g., OmpK35. OmpK36) and the need to optimize recombinant protein stability for therapeutic use. Overall, OmpK recombinant protein is a valuable tool for addressing antimicrobial resistance and developing novel infection control strategies.
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