| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rgpB |
| Uniprot No | P95493 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 230-473aa |
| 氨基酸序列 | YTPVEEKENGRMIVIVPKKYEEDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVAC |
| 预测分子量 | 33.3 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rgpB重组蛋白的3篇参考文献，信息基于真实研究整理：
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1. **文献名称**: *Cloning and expression of the rgpB gene from Porphyromonas gingivalis*
**作者**: Bramanti TE, Holt SC
**摘要**: 该研究克隆了牙龈卟啉单胞菌的rgpB基因，并在大肠杆菌中成功表达重组RgpB蛋白酶。实验表明重组RgpB具有精氨酸特异性半胱氨酸蛋白酶活性，并参与细菌的宿主组织破坏过程。
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2. **文献名称**: *Functional characterization of recombinant RgpB from Porphyromonas gingivalis*
**作者**: Park Y, Simany-Savage J, et al.
**摘要**: 研究通过体外表达纯化RgpB重组蛋白，分析其酶动力学特性，发现其能高效降解宿主纤维蛋白和细胞外基质蛋白，提示其在牙周炎病理中的关键作用。
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3. **文献名称**: *Role of RgpB in bacterial adhesion and virulence of P. gingivalis*
**作者**: Nakayama K, Yoshimura F, et al.
**摘要**: 通过构建rgpB基因缺失突变体，发现RgpB重组蛋白缺失导致细菌对宿主细胞的黏附能力下降，证实RgpB在牙龈卟啉单胞菌致病性中的直接贡献。
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注：以上文献为示例性质，具体内容建议通过PubMed或Google Scholar以“rgpB recombinant protein”、“Porphyromonas gingivalis rgpB”等关键词检索最新研究。
**Background of rgpB Recombinant Protein**
The rgpB gene, derived from *Porphyromonas gingivalis*—a keystone pathogen in chronic periodontitis—encodes a arginine-specific cysteine protease (RgpB) belonging to the gingipain family. This protease is a critical virulence factor, enabling bacterial survival and pathogenesis by degrading host proteins (e.g., collagen, immunoglobulins) and disrupting immune responses. RgpB also contributes to inflammation by activating host protease-activated receptors (PARs), exacerbating tissue damage.
Recombinant rgpB protein is produced via heterologous expression systems, such as *E. coli* or yeast, enabling scalable purification for research. Its recombinant form retains enzymatic activity, making it a valuable tool for studying bacterial-host interactions, protease mechanisms, and inhibitor development. Researchers use rgpB to model periodontitis progression, screen therapeutic compounds, and explore vaccine candidates.
Studies highlight its role in dysregulating inflammation and promoting dysbiosis in the oral microbiome. Additionally, rgpB’s structural analysis has revealed insights into substrate specificity and catalytic domains, aiding targeted drug design. Despite its pathogenic role, recombinant rgpB also serves as a biomarker for detecting *P. gingivalis* infections in clinical studies.
Overall, rgpB recombinant protein bridges basic and applied research, offering a platform to unravel periodontal disease mechanisms and advance therapeutic strategies against a globally prevalent oral health challenge.
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