| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | folA |
| Uniprot No | P99079 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-159aa |
| 氨基酸序列 | TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK |
| 预测分子量 | 25.6 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folA重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**: "Cloning, expression, and purification of functional recombinant folA gene product from *Escherichia coli*"
**作者**: Smith J, et al.
**摘要**: 该研究报道了通过克隆大肠杆菌folA基因，利用原核表达系统成功表达并纯化具有活性的重组二氢叶酸还原酶(DHFR)，验证了其酶动力学参数及对甲氧苄啶的敏感性。
2. **文献名称**: "Structural insights into the mechanism of antibiotic resistance in mutant folA recombinant proteins"
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了耐药性相关的folA突变体重组蛋白结构，揭示了关键氨基酸突变导致甲氧苄啶结合能力下降的分子机制。
3. **文献名称**: "Development of a high-yield recombinant folA protein production system in *Pichia pastoris* for enzymatic assays"
**作者**: Gonzalez R, et al.
**摘要**: 研究优化了毕赤酵母系统中重组folA蛋白的高效分泌表达策略，纯化蛋白适用于高通量酶活性筛选及抑制剂开发。
*注：以上文献信息为示例性质，实际文献需通过学术数据库检索确认。*
**Background of folA Recombinant Protein**
The *folA* gene encodes dihydrofolate reductase (DHFR), a critical enzyme in the folate biosynthesis pathway, which is essential for nucleotide synthesis and cellular metabolism. In bacteria, DHFR catalyzes the reduction of dihydrofolate to tetrahydrofolate (THF), a cofactor required for the synthesis of thymidylate, purines, and certain amino acids. Due to its pivotal role in DNA replication and cell proliferation, DHFR is a well-characterized target for antimicrobial agents, such as trimethoprim.
Recombinant folA protein is produced via genetic engineering, typically by cloning the *folA* gene into expression vectors (e.g., *E. coli* plasmids) and inducing protein production under controlled conditions. This allows large-scale purification of the enzyme for structural, functional, or pharmacological studies. The recombinant protein retains the enzymatic activity of native DHFR, making it invaluable for *in vitro* assays to study enzyme kinetics, inhibitor binding, or mechanisms of antibiotic resistance.
In research, folA recombinant protein is widely used to investigate bacterial folate metabolism and validate novel antimicrobial compounds. For instance, structural analyses of DHFR from pathogenic bacteria (e.g., *Mycobacterium tuberculosis* or *Staphylococcus aureus*) help design species-specific inhibitors. Additionally, mutations in *folA* linked to trimethoprim resistance are studied using recombinant variants to understand resistance mechanisms and optimize drug efficacy.
Beyond antimicrobial applications, folA recombinant protein serves as a model system in biochemistry for exploring protein folding, stability, and enzyme-substrate interactions. Its small size (~20 kDa) and well-defined structure facilitate computational and experimental studies. Furthermore, engineered DHFR variants with altered substrate specificity or enhanced stability are exploited in biotechnology, including molecular cloning and fusion protein systems.
Overall, folA recombinant protein is a versatile tool bridging basic science and drug development, with implications for combating infectious diseases and advancing enzymology research.
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