纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CNPY1 |
Uniprot No | Q3B7I2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-92aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL |
预测分子量 | 13 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CNPY1重组蛋白的3篇参考文献示例(注:文献为假设性示例,建议通过学术数据库查询真实研究):
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1. **文献名称**:*CNPY1 facilitates the assembly of the TLR4 signaling complex by bridging the UBC9 and TRIF components*
**作者**:Lee, J. et al. (2017)
**摘要**:研究通过表达重组CNPY1蛋白,发现其作为分子桥梁连接UBC9和TRIF蛋白,从而促进TLR4信号复合物的组装,增强先天免疫反应中NF-κB的激活。
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2. **文献名称**:*Recombinant CNPY1 promotes angiogenesis via enhancing VEGF receptor stability in endothelial cells*
**作者**:Wang, X. et al. (2018)
**摘要**:利用重组CNPY1蛋白处理内皮细胞,证实其通过结合VEGFR2并抑制泛素化降解,增强VEGF信号通路活性,促进血管新生及肿瘤生长。
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3. **文献名称**:*CNPY1 exacerbates atherosclerosis by inducing endoplasmic reticulum stress in macrophages*
**作者**:Chen, L. et al. (2020)
**摘要**:研究通过体外表达重组CNPY1蛋白,发现其诱导巨噬细胞内质网应激并促进炎症因子释放,加速动脉粥样硬化斑块形成。
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**建议**:可通过PubMed、Google Scholar等平台,以“CNPY1 recombinant protein”、“CNPY1 function”等关键词检索真实文献。
CNPY1 (Canopy FGF Signaling Regulator 1), also known as PRADC1. is a conserved member of the CNPY family of proteins primarily localized in the endoplasmic reticulum (ER). It plays a regulatory role in protein secretion and folding, particularly influencing the fibroblast growth factor (FGF) signaling pathway. CNPY1 is involved in modulating the biosynthesis and trafficking of secreted or membrane-bound proteins, such as Toll-like receptors (TLRs) and FGF receptors, by interacting with molecular chaperones like GRP94 in the ER. Structurally, it contains a signal peptide at its N-terminus and a conserved CNPY domain at the C-terminus, which mediates protein-protein interactions and oligomerization.
Recombinant CNPY1 protein is engineered through heterologous expression systems (e.g., *E. coli*, mammalian, or insect cells*) to study its biochemical functions and interactions. Purified recombinant CNPY1 retains its ability to bind chaperones and client proteins, making it a valuable tool for investigating ER-associated processes, including protein quality control, stress responses, and secretory pathway regulation. Studies have linked CNPY1 dysregulation to diseases such as cancer, inflammation, and metabolic disorders, highlighting its potential as a therapeutic target or biomarker. Its recombinant form is commonly utilized in *in vitro* assays, structural studies, and drug discovery platforms to dissect its role in cellular homeostasis and disease mechanisms.
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