纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | folP |
Uniprot No | Q59919 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-267aa |
氨基酸序列 | MTKTKIIGILNVTPDSFSDGGKYNSVDKAIARAKEMIDEGVDIIDVGGVSTRPGHTEVSLEEEMERVVPVVEQLVKLDVQISVDTYRSEVAEACLKLGATMINDQWAGLYDPKIFDVVSDYNAEIVLMHNGDGQREQPVVEEMLLSLLTQANKAEMAGIEKGNIWLDPGIGFAKSRSEEKEVMARLDELVATEYPVLLATSRKRFIKEMIGKETTPAERDEATAATTVYGIMKGIQAVRVHNVDLNVKLAQSIDFLKENEHERHHLS |
预测分子量 | 33.6 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 **folP重组蛋白** 的3篇假设性参考文献示例(实际文献需根据具体数据库检索):
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1. **文献名称**: *Cloning and characterization of recombinant folP from Streptococcus pneumoniae*
**作者**: Smith A, et al.
**摘要**: 本研究克隆并表达了肺炎链球菌的folP基因,获得重组蛋白,并测定其二氢蝶酸合成酶(DHPS)活性。发现某些氨基酸突变与磺胺类药物耐药性相关,为耐药机制提供了分子基础。
2. **文献名称**: *Crystal structure of recombinant FolP from Mycobacterium tuberculosis*
**作者**: Lee B, et al.
**摘要**: 通过X射线晶体学解析结核分枝杆菌folP重组蛋白的三维结构,揭示了其与磺胺类药物结合的活性位点,为新型抗菌剂设计提供了结构依据。
3. **文献名称**: *Functional analysis of folP homologs in pathogenic bacteria*
**作者**: Zhang C, et al.
**摘要**: 比较多种病原体中folP重组蛋白的酶动力学特性,发现不同菌株间酶活性和药物敏感性差异显著,提示叶酸通路在细菌适应性进化中的重要性。
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如需真实文献,建议在 **PubMed** 或 **Google Scholar** 中检索关键词:*recombinant folP protein*、*dihydropteroate synthase expression*。
**Background of FolP Recombinant Protein**
The *folP* gene encodes dihydropteroate synthase (DHPS), a key enzyme in the folate biosynthesis pathway of bacteria and some eukaryotes. Folate is essential for DNA synthesis and cell division, making DHPS a critical target for antimicrobial agents like sulfonamides. These drugs competitively inhibit DHPS by mimicking its substrate, para-aminobenzoic acid (pABA), thereby disrupting folate production and bacterial growth.
Recombinant FolP protein refers to the DHPS enzyme produced via genetic engineering techniques. This involves cloning the *folP* gene into expression vectors (e.g., plasmids), followed by protein expression in host systems like *E. coli* or yeast. The recombinant protein is then purified for functional and structural studies. Its production enables detailed analysis of enzyme kinetics, substrate specificity, and interactions with inhibitors, which are vital for understanding antibiotic resistance mechanisms.
Interest in FolP recombinant protein stems from its role in addressing antimicrobial resistance (AMR). Mutations in *folP* associated with sulfonamide resistance (e.g., in *Streptococcus pneumoniae* or *Staphylococcus aureus*) reduce drug binding efficiency. Studying recombinant variants helps identify resistance patterns and design next-generation inhibitors. Additionally, FolP is explored as a vaccine candidate in pathogens like *Mycobacterium tuberculosis*, where folate pathway proteins may elicit protective immune responses.
Beyond therapeutics, FolP recombinant proteins are used in diagnostics to detect sulfonamide resistance markers and in synthetic biology for engineering folate-dependent pathways. Overall, FolP research bridges microbiology, structural biology, and drug development, offering insights into combating infectious diseases in an era of rising AMR.
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