| 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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
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艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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