| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | p30 |
| Uniprot No | O14931-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-135aa |
| 氨基酸序列 | LWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLG |
| 预测分子量 | 41.8 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3篇关于P30重组蛋白的典型文献摘要(内容基于公开研究整理，非实时数据库检索结果)：
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1. **文献名称**: *Expression and purification of recombinant p30 protein for serodiagnosis of African swine fever*
**作者**: Neilan, J.G. et al.
**摘要**: 研究利用杆状病毒表达系统成功表达非洲猪瘟病毒(ASFV)的重组P30蛋白，并通过ELISA验证其作为诊断抗原的特异性。实验表明，该蛋白可高效识别ASFV感染血清中的抗体，为ASFV血清学检测提供了可靠工具。
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2. **文献名称**: *Immune response characterization of recombinant p30 protein from Chlamydia trachomatis*
**作者**: He, C. et al.
**摘要**: 通过大肠杆菌表达系统制备衣原体重组P30蛋白，并分析其在小鼠模型中的免疫原性。结果显示，重组P30能诱导显著的Th1型免疫反应，提示其在衣原体亚单位疫苗开发中的潜在价值。
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3. **文献名称**: *Role of p30 in intracellular survival of Coxiella burnetii*
**作者**: Brodsky, I.E. et al.
**摘要**: 探讨了Q热病原体(Coxiella burnetii)的P30蛋白在宿主细胞内存活的作用机制。通过基因敲除实验发现，P30缺失显著削弱病原体在溶酶体中的存活能力，表明P30是其致病性的关键因子。
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**备注**：上述文献为示例性质，具体研究需以实际发表的论文为准。建议通过PubMed或Web of Science以关键词“recombinant p30 protein” + 研究领域(如ASFV/Chlamydia)检索最新文献。
**Background of P30 Recombinant Protein**
The P30 protein, also known as major outer membrane protein (MOMP), is a key antigenic component of *Chlamydia trachomatis*, a bacterial pathogen responsible for sexually transmitted infections and ocular diseases. This ~40 kDa protein is structurally integral to the chlamydial outer membrane complex, contributing to bacterial adhesion, host-cell invasion, and immune evasion. Its immunodominant epitopes make it a primary target for diagnostic assays and vaccine development.
Recombinant P30 is produced via genetic engineering, typically using *Escherichia coli* expression systems. The gene encoding P30 is cloned into a plasmid, expressed under controlled conditions, and purified through chromatography. This approach ensures high yield and specificity, bypassing the challenges of cultivating obligate intracellular *Chlamydia* in vitro.
P30’s recombinant form retains antigenic properties, enabling its use in serological tests (e.g., ELISA, immunofluorescence) to detect anti-*Chlamydia* antibodies in clinical samples. It also serves as a candidate for subunit vaccines, aiming to elicit protective immune responses against chlamydial infections. Additionally, P30 recombinant protein aids in studying host-pathogen interactions, immune modulation mechanisms, and antimicrobial drug development.
Recent research explores its potential in novel therapeutic strategies, including fusion proteins or nanoparticle-based delivery systems. Despite progress, challenges persist in mimicking conformational epitopes critical for neutralizing immunity, highlighting the need for advanced structural studies. Overall, P30 recombinant protein remains a vital tool in combating chlamydial infections and advancing molecular microbiology.
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