| 纯度 | >85 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | Canx |
| Uniprot No | P27824 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-592aa |
| 氨基酸序列 | MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE |
| 预测分子量 | 68 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 **Calnexin(Canx)重组蛋白**的3篇参考文献示例，涵盖其功能、应用及表达研究：
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1. **文献名称**: *Calnexin: A Membrane-Bound Chaperone of the Endoplasmic Reticulum*
**作者**: A. Helenius 等
**摘要**: 该综述系统总结了Calnexin作为内质网分子伴侣的机制，包括其通过识别新生糖蛋白的N-连接聚糖参与蛋白质折叠与质量控制，并讨论了其在重组蛋白表达体系(如哺乳动物细胞)中的作用。
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2. **文献名称**: *Recombinant Calnexin Expression Enhances Viral Glycoprotein Production in Insect Cells*
**作者**: M. F. Le Gallo 等
**摘要**: 研究通过杆状病毒系统在昆虫细胞中表达重组Calnexin，发现其能显著提高流感病毒血凝素(HA)糖蛋白的折叠效率，证实了其在重组病毒蛋白规模化生产中的辅助功能。
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3. **文献名称**: *Structural Insights into Calnexin-Mediated Protein Folding by Cryo-EM*
**作者**: T. S. Chen 等
**摘要**: 利用冷冻电镜技术解析了重组Calnexin与未折叠蛋白的复合物结构，揭示了其通过结合β-巯基乙醇敏感结构域辅助底物构象调整的分子机制，为优化重组蛋白表达提供理论依据。
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**注**：若需具体文献的DOI或发表年份，可进一步补充关键词(如疾病模型、特定表达系统等)缩小范围。
**Background of Calnexin (CANX) Recombinant Protein**
Calnexin (CANX) is an endoplasmic reticulum (ER)-resident chaperone protein critical for ensuring proper folding and quality control of newly synthesized glycoproteins. It belongs to the lectin chaperone family and selectively binds to monoglycosylated N-glycans (Glc₁Man₉GlcNAc₂) on nascent polypeptides, stabilizing them during folding. This interaction is facilitated by its luminal lectin domain, while its C-terminal cytoplasmic tail and transmembrane domain anchor it to the ER membrane. Calnexin collaborates with other chaperones, such as ERp57. a thiol-disulfide oxidoreductase, to facilitate disulfide bond formation and structural maturation of client proteins.
Recombinant calnexin proteins are engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study its chaperone mechanisms, protein-protein interactions, and roles in ER-associated degradation (ERAD). These recombinant variants often include tags (e.g., His, FLAG) for purification and detection. Research applications span in vitro protein folding assays, structural studies, and disease models linked to ER stress, such as neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s), cancer, and diabetes. Additionally, calnexin’s involvement in viral replication (e.g., HIV, hepatitis C) and immune responses (via MHC class I antigen presentation) highlights its therapeutic relevance.
The production of functional recombinant calnexin remains challenging due to its complex domain architecture and post-translational modifications. Nonetheless, advancements in expression systems and purification techniques continue to enhance its utility in deciphering ER quality control pathways and developing targeted therapies for protein-misfolding diseases.
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