| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OBP2A |
| Uniprot No | Q9NY56 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-170aa |
| 氨基酸序列 | LSFTLEEEDITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGNLEATFTFMREDRCIQKKILMRKTEEPGKFSAYGGRKLIYLQELPGTDDYVFYSKDQRRGGLRYMGNLVGRNPNTNLEALEEFKKLVQHKGLSEEDIFMPLQTGSCVLEH |
| 预测分子量 | 30.8 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. |
以下是关于OBP2A重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Expression and characterization of a recombinant odorant-binding protein 2A (OBP2A) from the mosquito Anopheles gambiae*
**作者**：Tsuchihara-Ito, K., et al.
**摘要**：该研究利用大肠杆菌系统成功表达并纯化了疟蚊Anopheles gambiae的OBP2A重组蛋白，分析了其在体外与特定气味分子的结合能力，揭示了其在嗅觉信号传导中的潜在作用。
2. **文献名称**：*Structural and functional analysis of OBP2A in Drosophila melanogaster*
**作者**：Zhu, J., et al.
**摘要**：通过X射线晶体学解析了果蝇OBP2A的三维结构，并证明其通过疏水口袋选择性结合挥发性化合物，为理解昆虫化学感受机制提供了结构基础。
3. **文献名称**：*Recombinant OBP2A as a potential biosensor for volatile organic compounds*
**作者**：Sun, Y., et al.
**摘要**：开发了一种基于OBP2A重组蛋白的生物传感器，可高效检测环境中的苯类挥发性物质，验证了其在环境监测中的应用潜力。
**备注**：上述文献为示例性质，实际发表情况需通过学术数据库(如PubMed、Web of Science)核实。建议结合关键词“OBP2A recombinant protein”或“odorant-binding protein expression”检索最新研究。
**Background of OBP2A Recombinant Protein**
Odorant-binding protein 2A (OBP2A) belongs to a family of small, soluble extracellular proteins critical for chemosensory perception in insects. These proteins facilitate the detection and transport of hydrophobic odorant molecules, such as pheromones or environmental volatiles, to olfactory receptors in sensory organs. OBP2A, specifically, is studied for its role in mediating insect-host interactions, including feeding, mating, and habitat selection, making it a potential target for pest control strategies.
The production of recombinant OBP2A leverages genetic engineering to express and purify the protein *in vitro*, typically using bacterial (e.g., *E. coli*) or insect cell expression systems. This approach allows large-scale production of functional OBP2A for structural and functional studies. Researchers employ techniques like X-ray crystallography or NMR spectroscopy to elucidate its ligand-binding specificity and conformational dynamics, providing insights into how it interacts with specific odorants.
Beyond basic research, recombinant OBP2A has applications in developing eco-friendly pest management tools. For example, disrupting OBP2A function could impair insect olfactory signaling, reducing their ability to locate hosts or mates. Additionally, OBP2A-based biosensors are explored for environmental monitoring or detecting volatile organic compounds.
Studies on OBP2A also contribute to understanding evolutionary adaptations in insect olfaction across species, highlighting conserved or divergent mechanisms in chemical communication. Overall, recombinant OBP2A serves as a versatile tool for both academic research and applied biotechnology, bridging gaps between molecular biology, ecology, and sustainable agriculture.
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