| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OmpK36 |
| Uniprot No | Q48473 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-363aa |
| 氨基酸序列 | MKVKVLSLLVPALLVAGAANAAEIYNKDGNKLDLYGKIDGLHYFSDDKDVDGDQTYMRLGVKGETQINDQLTGYGQWEYNVQANNTESSSDQAWTRLAFAGLKFGDAGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFLQSRANGVATYRNSDFFGLVDGLNFALQYQGKNGSVSGEGATNNGRGALKQNGDGFGTSVTYDIFDGISAGFAYANSKRTDDQNQLLLGEGDHAETYTGGLKYDANNIYLATQYTQTYNATRAGSLGFANKAQNFEVAAQYQFDFGLRPSVAYLQSKGKDLNGYGDQDILKYVDVGATYYFNKNMSTYVDYKINLLDDNSFTRSAGISTDDVVALGLVYQF |
| 预测分子量 | 39,6 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OmpK36重组蛋白的3篇参考文献示例(注：以下文献信息为模拟虚构，仅供参考格式)：
1. **文献名称**: *"Role of OmpK36 porin in antimicrobial resistance of Klebsiella pneumoniae"*
**作者**: Lee JH, et al.
**摘要**: 本研究通过克隆表达OmpK36重组蛋白，分析其孔道蛋白功能与碳青霉烯类抗生素耐药性的关系，发现OmpK36的结构突变显著降低外膜通透性，导致菌株对美罗培南的敏感性下降。
2. **文献名称**: *"Expression and purification of recombinant OmpK36 for structural characterization"*
**作者**: Zhang Y, et al.
**摘要**: 报道了OmpK36基因在大肠杆菌中的高效表达及纯化方法，利用X射线晶体学解析其三维结构，揭示其孔道区域的关键氨基酸残基可能与抗生素结合相关。
3. **文献名称**: *"Immunogenicity of recombinant OmpK36 as a vaccine candidate against Klebsiella infections"*
**作者**: Gupta S, et al.
**摘要**: 评估了重组OmpK36蛋白在小鼠模型中的免疫保护效果，结果显示其能诱导高滴度抗体并增强宿主对肺炎克雷伯菌感染的清除能力，表明其作为疫苗靶标的潜力。
如需真实文献，建议通过PubMed或Google Scholar搜索关键词“OmpK36 recombinant protein”获取具体研究。
OmpK36 is an outer membrane porin protein primarily found in Gram-negative bacteria, particularly within the Enterobacteriaceae family, such as *Klebsiella pneumoniae* and *Escherichia coli*. As a member of the porin family, it forms β-barrel channels in the bacterial outer membrane, facilitating the passive diffusion of small hydrophilic molecules, including nutrients and antimicrobial agents. Structurally, OmpK36 consists of 16 β-strands forming a transmembrane barrel, with extracellular loops (notably loops L3 and L6) modulating pore size and solute selectivity.
The protein has gained attention due to its role in antibiotic resistance. Under selective pressure from β-lactams or quinolones, bacteria often downregulate or mutate OmpK36. reducing membrane permeability and limiting drug uptake. For instance, truncated or modified L3 loops in OmpK36 are linked to carbapenem resistance in *K. pneumoniae*. This adaptive mechanism underscores its clinical relevance in multidrug-resistant infections.
Recombinant OmpK36 is produced via heterologous expression systems (e.g., *E. coli*) for functional and structural studies. Cloning the *ompK36* gene into expression vectors allows large-scale protein production, often purified via affinity chromatography (e.g., His-tag systems). Studies leveraging recombinant OmpK36 aim to elucidate pore dynamics, substrate specificity, and interactions with antibiotics or host immune components. Additionally, it serves as a potential vaccine candidate or diagnostic marker due to its surface exposure and antigenicity.
Recent structural analyses (X-ray crystallography, cryo-EM) have resolved conformational changes during pore gating, informing drug design strategies to bypass porin-mediated resistance. Research on recombinant OmpK36 continues to bridge gaps in understanding bacterial adaptation mechanisms and developing therapeutic countermeasures.
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