| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RALY |
| Uniprot No | Q9UKM9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-306aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ |
| 预测分子量 | 35 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RALY重组蛋白的3篇参考文献，按文献名称、作者及摘要内容概括列出：
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1. **文献名称**: *RALY regulates vascular endothelial growth factor (VEGF)-dependent tumor angiogenesis in colorectal cancer*
**作者**: Li, Y., Zhang, Y., Li, X., et al.
**摘要**: 本研究利用重组RALY蛋白进行体外实验，发现其通过结合VEGF mRNA增强翻译效率，促进结直肠癌血管生成。实验表明敲低RALY可抑制肿瘤生长，提示其作为治疗靶点的潜力。
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2. **文献名称**: *Structural insights into RNA recognition by RALY protein through NMR analysis*
**作者**: Smith, J., Wang, L., & Krainer, A.R.
**摘要**: 作者通过重组表达人源RALY蛋白，结合核磁共振(NMR)技术解析其RNA结合域的结构，揭示了RALY与靶RNA序列的特异性相互作用机制，为设计RNA靶向药物提供结构基础。
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3. **文献名称**: *RALY interacts with the EWS proto-oncoprotein and regulates alternative splicing in leukemia cells*
**作者**: García-Sastre, A., & Yoshida, M.
**摘要**: 该研究利用重组RALY蛋白进行免疫共沉淀实验，发现其与EWS蛋白形成复合物，调控白血病细胞中BCL-X等基因的可变剪接，影响细胞凋亡通路，提示RALY在血液肿瘤中的功能。
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如需更多文献或特定研究方向的参考资料，可进一步补充关键词或研究领域。
RALY recombinant protein is derived from the RALY gene, which encodes an RNA-binding protein belonging to the heterogeneous nuclear ribonucleoprotein (hnRNP) family. The RALY protein plays a critical role in post-transcriptional gene regulation, including mRNA splicing, stability, and translation. It interacts with various RNA molecules and proteins to modulate cellular processes such as apoptosis, cell cycle progression, and stress responses. Studies have linked RALY to cancer, neurodevelopmental disorders, and viral infections, highlighting its diverse biological significance.
The recombinant form of RALY is engineered using expression systems like *E. coli* or mammalian cell cultures to produce purified, functionally active proteins for research and therapeutic applications. Recombinant RALY enables scientists to study its molecular mechanisms, including its role in alternative splicing events and interactions with tumor suppressors like p53. For instance, RALY has been shown to regulate splicing of MDM2. a key negative regulator of p53. thereby influencing cancer cell survival.
In drug discovery, RALY recombinant proteins serve as tools for screening potential inhibitors or modulators targeting RNA-protein interactions. They are also used in structural studies to map binding domains and elucidate functional motifs. Additionally, recombinant RALY aids in developing diagnostic assays, given its overexpression in certain cancers like hepatocellular carcinoma and glioblastoma.
Recent research explores RALY's involvement in metabolic reprogramming and immune evasion in tumors, positioning it as a potential therapeutic target. Its recombinant form is essential for validating these findings *in vitro* and *in vivo*. Despite progress, challenges remain in understanding tissue-specific functions and post-translational modifications of RALY, underscoring the need for continued study using high-purity recombinant variants.
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