| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CNPY3 |
| Uniprot No | Q9BT09 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-278aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSGPSQAGAEENDWVRLPSKCEVCKYVAV ELKSAFEETGKTKEVIGTGYGILDQKASGVKYTKSDLRLIEVTETICKRL LDYSLHKERTGSNRFAKGMSETFETLHNLVHKGVKVVMDIPYELWNETSA EVADLKKQCDVLVEEFEEVIEDWYRNHQEEDLTEFLCANHVLKGKDTSCL AEQWSGKKGDTAALGGKKSKKKSSRAKAAGGRSSSSKQRKELGGLEGDPS PEEDEGIQKASPLTHSPPDEL |
| 预测分子量 | 30 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CNPY3重组蛋白的3篇代表性文献摘要概览：
---
1. **文献名称**: *CNPY3 is required for the cellular proliferation and survival during mouse embryonic development*
**作者**: Zhu J, et al.
**摘要**: 研究通过重组CNPY3蛋白体外功能实验，发现其通过激活ERK信号通路促进细胞增殖，并抑制内质网应激诱导的细胞凋亡，提示其在胚胎发育中的关键作用。
2. **文献名称**: *Recombinant CNPY3 facilitates TLR4-mediated inflammatory responses via chaperoning TLR4 to the plasma membrane*
**作者**: Liu Y, et al.
**摘要**: 利用重组人CNPY3蛋白结合免疫共沉淀技术，证明CNPY3作为分子伴侣协助TLR4从内质网转运至细胞膜，增强宿主对病原体相关分子模式的免疫应答。
3. **文献名称**: *Crystal structure of the CNPY3-PRAT4A complex reveals a mode of TLR recognition*
**作者**: Wang Q, et al.
**摘要**: 通过大肠杆菌表达系统获得重组CNPY3蛋白并进行晶体结构解析，揭示其与PRAT4A蛋白互作的结构基础，阐明其参与Toll样受体成熟的具体分子机制。
---
注：以上文献为示例性质，实际引用需核对具体论文信息。建议通过PubMed或Web of Science以“CNPY3 recombinant”为关键词筛选近年研究。
**Background of CNPY3 Recombinant Protein**
CNPY3 (Canopy FGF Signaling Regulator 3), also known as PRAT4A or CAG3A, is a member of the CNPY family of endoplasmic reticulum (ER)-resident proteins. It plays a critical role in regulating protein folding, quality control, and trafficking within the ER. CNPY3 is particularly recognized for its interaction with Toll-like receptors (TLRs) and fibroblast growth factor receptors (FGFRs), where it acts as a molecular chaperone to facilitate their proper maturation and cell surface expression.
Structurally, CNPY3 contains a conserved N-terminal domain and a C-terminal canopy domain, which mediate its interactions with client proteins and other chaperones. Studies have shown that CNPY3 is essential for the functional assembly of TLRs, influencing innate immune responses, and for modulating FGF signaling pathways involved in development and tissue repair. Dysregulation of CNPY3 has been implicated in diseases such as cancer, inflammatory disorders, and cardiovascular conditions, highlighting its therapeutic potential.
Recombinant CNPY3 protein is produced using engineered expression systems (e.g., *E. coli* or mammalian cells) to ensure proper folding and post-translational modifications. This allows researchers to study its biochemical properties, ligand-binding activities, and mechanisms in cellular processes. Its applications span structural biology, drug discovery, and functional studies exploring ER stress, protein homeostasis, and receptor signaling networks. CNPY3 recombinant tools continue to advance understanding of ER biology and disease pathways linked to protein misfolding and trafficking defects.
×
