纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RASSF5 |
Uniprot No | Q8WWW0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-265aa |
氨基酸序列 | MTVDSSMSSGYCSLDEELEDCFFTAKTTFFRNAQSKHLSKNVCKPVEETQRPPTLQEIKQKIDSYNTREKNCLGMKLSEDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYDAIKEVNLAATTDKRTSFYLPLDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRIHKDGQVLFQKLSIADRPLYLRLLAGPDTEVLSFVLKENETGEVEWDAFSIPELQNFLTILEKEEQDKIQQVQKKYDKFRQKLEEALRESQGKPG |
预测分子量 | 57.4 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RASSF5重组蛋白的3篇参考文献的简要总结(基于公开研究内容归纳,非真实文献):
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1. **文献名称**:*RASSF5 (NORE1A) interacts with MST1/2 kinases to regulate apoptosis through the Hippo pathway*
**作者**:Guo, C., Tommasi, S., et al.
**摘要**:该研究利用重组RASSF5蛋白,揭示了其通过结合Hippo通路激酶MST1/2.调控细胞凋亡的分子机制。体外实验表明,重组RASSF5可增强MST1对下游靶点的磷酸化,抑制肿瘤细胞生长。
2. **文献名称**:*Structural and functional analysis of RASSF5 effector interactions*
**作者**:Richter, A. M., & Pfeifer, G. P.
**摘要**:通过大肠杆菌表达系统纯化重组RASSF5蛋白,结合X射线晶体学解析其三维结构,并证明其通过RA结构域与Ras蛋白结合,参与MAPK信号通路的负调控。
3. **文献名称**:*NORE1A (RASSF5) suppresses oncogenic cell transformation by promoting KRAS degradation*
**作者**:Vos, M. D., et al.
**摘要**:研究利用HEK293细胞表达的重组RASSF5蛋白,发现其通过泛素-蛋白酶体途径促进致癌KRAS蛋白的降解,从而抑制肿瘤发生,为RASSF5的抑癌功能提供了生化证据。
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**备注**:以上文献为示例性质,实际引用时需查询具体论文数据库(如PubMed)获取真实文献信息。
**Background of RASSF5 Recombinant Protein**
RASSF5 (Ras Association Domain Family Member 5), also known as RAPL or NORE1. is a member of the RASSF tumor suppressor protein family, which plays critical roles in regulating cell proliferation, apoptosis, and immune responses. It is encoded by the *RASSF5* gene and exists in multiple isoforms, including a long isoform (NORE1A/RAPL) and a shorter splice variant (NORE1B), differing in their C-terminal regions. RASSF5 functions as a scaffold protein, mediating interactions between key signaling molecules, particularly those in the Hippo and Ras pathways.
Structurally, RASSF5 contains a conserved Ras-association (RA) domain at its N-terminus, enabling direct binding to activated Ras GTPases, and a Salvador/RASSF/Hippo (SARAH) domain at the C-terminus, facilitating dimerization and interaction with downstream effectors like MST1/2 kinases. Recombinant RASSF5 proteins are engineered to study these interactions, often expressed in bacterial or mammalian systems to ensure proper post-translational modifications.
Functionally, RASSF5 acts as a tumor suppressor by promoting apoptosis and cell cycle arrest through Hippo pathway activation and p53 stabilization. It also regulates immune cell activity, particularly T-cell adhesion and dendritic cell maturation. Studies show that RASSF5 knockout mice exhibit defective immune synapse formation and impaired lymphocyte migration. Dysregulation of RASSF5. due to promoter hypermethylation or mutations, is linked to cancers, including lung, breast, and colorectal malignancies.
Recombinant RASSF5 is widely used in research to explore its tumor-suppressive mechanisms, interactions with oncogenic Ras mutants, and role in immune regulation. It serves as a tool for identifying therapeutic targets, such as small molecules to restore RASSF5 function in cancers or modulate immune responses in autoimmune diseases. Additionally, recombinant RASSF5 aids in structural studies to map binding interfaces critical for signaling, offering insights into designing pathway-specific inhibitors or activators.
In summary, RASSF5 recombinant protein is pivotal for dissecting its dual role in tumor suppression and immune modulation, bridging basic research with potential clinical applications.
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