| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPFL9 |
| Uniprot No | Q9SV72 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-102aa |
| 氨基酸序列 | SRPRSIENTVSLLPQVHLLNSRRRHMIGSTAPTCTYNECRGCRYKCRAEQVPVEGNDPINSAYHYRCVCHR |
| 预测分子量 | 10.2 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EPFL9重组蛋白的假设性参考文献示例(具体文献需根据实际研究核实)：
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1. **Title**: *EPFL9 regulates stomatal patterning through receptor kinase signaling in Arabidopsis*
**Authors**: Lee, J., Hara, K., & Torii, K.U.
**Summary**: 研究揭示了EPFL9作为分泌肽通过ERECTA受体激酶调控拟南芥气孔发育的分子机制，重组EPFL9蛋白体外实验证实其与受体互作并激活下游信号通路。
2. **Title**: *Heterologous expression and functional analysis of EPFL9 in plant drought resistance*
**Authors**: Zhang, Y., Wang, L., & Chen, Z.
**Summary**: 通过大肠杆菌系统表达重组EPFL9蛋白，验证其调控气孔关闭的功能，证明外源施加EPFL9可增强植物抗旱性，为作物改良提供新策略。
3. **Title**: *Structural characterization of EPFL9 peptide and its interaction with signaling components*
**Authors**: Tanaka, H., Sasaki, N., & Shinozaki, K.
**Summary**: 采用核磁共振解析重组EPFL9蛋白的三维结构，揭示其与受体激酶LOV域的相互作用界面，为设计气孔调控合成肽奠定基础。
4. **Title**: *CRISPR-based engineering of EPFL9 secretion efficiency in plant cells*
**Authors**: Müller, A., Dubiella, U., & Hothorn, M.
**Summary**: 通过优化重组EPFL9的分泌信号肽序列，提升其在烟草瞬时表达系统中的分泌效率，并验证其生物活性。
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**注意**：以上为基于EPF/EPFL家族蛋白研究的假设性示例，实际文献需通过PubMed/Google Scholar检索关键词(如“EPFL9 recombinant protein”、“EPFL9 stomatal development”)获取。若研究较少，可扩展至EPF/EPFL家族其他成员(如EPF1/EPF2)的相关文献。
EPFL9 is a member of the EPIDERMAL PATTERNING FACTOR-LIKE (EPFL) family, a group of small secreted cysteine-rich proteins in plants. These proteins play critical roles in regulating developmental processes and stress responses by modulating cell-to-cell communication. EPFL9. specifically, has been studied in the context of plant growth regulation, particularly in Arabidopsis thaliana. It functions as a signaling peptide that interacts with receptor kinases, such as those in the ERECTA family, to coordinate tissue patterning and organ development.
Structurally, EPFL9 contains conserved cysteine residues that form disulfide bonds, stabilizing its tertiary structure and enabling interaction with target receptors. Its secretion is mediated by an N-terminal signal peptide, a hallmark of extracellular signaling molecules. Studies suggest EPFL9 is involved in fine-tuning stomatal development, vascular differentiation, and inflorescence architecture, though its exact mechanistic role remains under investigation. Unlike some EPFL members with well-defined functions (e.g., EPF1/2 in stomatal patterning), EPFL9 appears to have overlapping or context-dependent roles, potentially acting as a redundant or compensatory signaling component.
Recombinant EPFL9 protein is typically produced in heterologous systems like Escherichia coli or yeast for functional studies. Purified EPFL9 is used to explore ligand-receptor interactions, signaling pathways, and phenotypic effects in planta. Its recombinant form has applications in agricultural biotechnology, such as engineering crops with optimized growth traits or stress resilience. Current research focuses on deciphering its spatiotemporal expression patterns, post-translational modifications, and cross-talk with other signaling networks to harness its potential for improving plant productivity.
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