| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CNPY2 |
| Uniprot No | Q9Y2B0-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-178aa |
| 氨基酸序列 | MKGWGWLALL LGALLGTAWA RRSQDLHCGA CRALVDELEW EIAQVDPKKT IQMGSFRINP DGSQSVVEVP YARSEAHLTE LLEEICDRMK EYGEQIDPST HRKNYVRVVG RNGESSELDL QGIRIDSDIS GTLKFACESI VEEYEDELIE FFSREADNVK DKLCSKRTDL CDHALHIS |
| 预测分子量 | 20 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CNPY2重组蛋白的3篇假设性参考文献示例(注：以下内容为模拟创作，实际文献需通过学术数据库查询确认)：
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1. **文献名称**: *CNPY2 promotes tumor angiogenesis via enhancing VEGF signaling in colorectal cancer*
**作者**: Zhang Y, et al.
**摘要**: 研究通过重组CNPY2蛋白体外实验，发现其可增强血管内皮生长因子(VEGF)信号通路，促进结直肠癌血管生成。重组蛋白通过大肠杆菌表达系统纯化，并验证了其与VEGFR2的相互作用。
2. **文献名称**: *Recombinant CNPY2 modulates ER stress response in neurodegenerative models*
**作者**: Li X, et al.
**摘要**: 该研究利用昆虫细胞表达系统制备重组CNPY2蛋白，发现其通过调控内质网(ER)未折叠蛋白反应，减轻帕金森病模型中的神经元损伤，提示其潜在神经保护作用。
3. **文献名称**: *Structural and functional analysis of CNPY2 in TLR4 signaling*
**作者**: Wang H, et al.
**摘要**: 通过重组CNPY2蛋白的晶体结构解析，揭示其与TLR4受体的结合模式，证明其在先天免疫反应中的调控功能，为炎症性疾病治疗提供新靶点。
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如需真实文献，建议使用PubMed或Google Scholar检索关键词 **"CNPY2 recombinant protein"** 或 **"CNPY2 expression function"**，并筛选近年研究。
CNPY2 (Canopy FGF Signaling Regulator 2), a member of the CNPY family, is an endoplasmic reticulum (ER)-resident protein implicated in regulating cellular stress responses, protein folding, and signaling pathways. Initially identified as a secreted glycoprotein, CNPY2 is evolutionarily conserved and ubiquitously expressed across tissues, with elevated levels observed in the liver, kidney, and immune cells. Structurally, it features an N-terminal signal peptide, a conserved canopy domain, and a C-terminal region rich in cysteine residues, which may facilitate disulfide bond formation and protein interactions.
Functionally, CNPY2 acts as a molecular chaperone or co-chaperone, aiding in the folding and maturation of client proteins within the ER. It interacts with key components of the unfolded protein response (UPR), modulating ER stress adaptation and apoptosis. Notably, CNPY2 has been linked to fibroblast growth factor (FGF) signaling, where it enhances FGF receptor stability and trafficking, influencing cell proliferation, differentiation, and tissue repair. Dysregulation of CNPY2 is associated with pathological conditions, including cancer, inflammatory diseases, and metabolic disorders. For instance, it is overexpressed in certain tumors, promoting angiogenesis and metastasis, while its deficiency correlates with impaired immune responses.
Recombinant CNPY2 protein, typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, retains bioactivity for *in vitro* studies. Purification often involves affinity tags (e.g., His-tag) and refolding steps to ensure proper conformation. This recombinant tool enables mechanistic exploration of CNPY2’s roles in protein-protein interactions, ER stress assays, and drug screening. Its therapeutic potential is being investigated, particularly in targeting ER stress-related diseases or modulating FGF signaling pathways for regenerative medicine. However, conflicting reports on its pro- or anti-apoptotic roles underscore the need for further research to clarify context-dependent functions.
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