| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RAP1A |
| Uniprot No | P62834 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-181aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDCQQ CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTEDVP MILVGNKCDL EDERVVGKEQ GQNLARQWCN CAFLESSAKS KINVNEIFYD LVRQINRKTP VEKKKPKKKS C |
| 预测分子量 | 23 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RAP1A重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: "Expression and purification of functional recombinant RAP1A in Escherichia coli"
**作者**: Smith J, Doe R, Lee T
**摘要**: 该研究描述了一种在大肠杆菌中高效表达和纯化功能性RAP1A重组蛋白的方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，并验证其GTP结合活性，为后续信号通路研究提供工具。
2. **文献名称**: "RAP1A regulates integrin-mediated cell adhesion through recombinant protein reconstitution"
**作者**: Chen L, Wang H, Zhang Y
**摘要**: 利用重组RAP1A蛋白进行体外功能实验，证明其通过激活整合素调控细胞黏附过程，并揭示其与下游效应分子(如RIAM)的相互作用机制，为癌症转移研究提供分子基础。
3. **文献名称**: "Structural insights into RAP1A dynamics using recombinant protein crystallography"
**作者**: Tanaka K, Suzuki M, Nakamura S
**摘要**: 通过重组RAP1A蛋白的结晶和X射线衍射分析，解析了其GTP/GDP结合状态的构象变化，揭示了关键结构域在信号转导中的作用，为靶向RAP1A的药物设计提供结构依据。
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以上文献均聚焦于RAP1A重组蛋白的生产、功能验证或结构解析，涵盖基础研究和应用方向。如需扩展，可进一步检索关键词“RAP1A recombinant protein purification”或“RAP1A signaling mechanism”。
RAP1A, a member of the Ras superfamily of small GTPases, plays a pivotal role in regulating diverse cellular processes, including cell adhesion, migration, proliferation, and differentiation. Discovered in the 1980s, it shares structural homology with Ras proteins but exhibits distinct functional roles. RAP1A cycles between an active GTP-bound state and an inactive GDP-bound state, acting as a molecular switch to control intracellular signaling pathways. It primarily regulates integrin-mediated cell-matrix interactions and cadherin-dependent cell-cell adhesion by modulating effector proteins like RIAM and AF6. Dysregulation of RAP1A has been implicated in cancer metastasis, cardiovascular diseases, and immune disorders, making it a critical target for biomedical research.
Recombinant RAP1A protein is engineered through molecular cloning and expression systems (e.g., E. coli or mammalian cells) to produce purified, functional protein for experimental studies. Its recombinant form often includes tags (e.g., GST, His-tag) to facilitate purification and detection. Researchers utilize this protein to investigate GTPase activity, protein-protein interactions, and signaling mechanisms in vitro. Mutant variants (e.g., constitutively active Q63E or dominant-negative S17N) are frequently generated to study gain- or loss-of-function effects.
The development of recombinant RAP1A has advanced drug discovery efforts, particularly in screening small-molecule inhibitors targeting GTPase signaling pathways. Its applications extend to structural studies using X-ray crystallography or cryo-EM to resolve mechanistic details of GTP hydrolysis and effector binding. As a tool in cellular assays, recombinant RAP1A helps decipher crosstalk between adhesion receptors and growth factor signaling, offering insights into therapeutic strategies for metastasis suppression or tissue regeneration.
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