| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CDC37L1 |
| Uniprot No | Q7L3B6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-337aa |
| 氨基酸序列 | MEQPWPPPGP WSLPRAEGEA EEESDFDVFP SSPRCPQLPG GGAQMYSHGI ELACQKQKEF VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAV SELRQREEEW RQKEEALVQR EKMCLWSTDA ISKDVFNKSF INQDKRKDTE DEDKSESFMQ KYEQKIRHFG MLSRWDDSQR FLSDHPYLVC EETAKYLILW CFHLEAEKKG ALMEQIAHQA VVMQFIMEMA KNCNVDPRGC FRLFFQKAKA EEEGYFEAFK NELEAFKSRV RLYSQSQSFQ PMTVQNHVPH SGVGSIGLLE SLPQNPDYLQ YSISTALCSL NSVVHKEDDE PKMMDTV |
| 预测分子量 | 38,8 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CDC37L1重组蛋白的3篇代表性文献示例(注：文献信息为模拟示例，非真实存在)：
---
1. **文献名称**：*CDC37L1 regulates HSP90-mediated protein folding through a tissue-specific chaperone complex*
**作者**：Zhang Y, et al.
**摘要**：本研究通过重组CDC37L1蛋白发现其与HSP90形成不同于CDC37的复合物，选择性辅助激酶客户蛋白的构象成熟，并在小鼠肝脏发育中调控MAPK信号通路。
2. **文献名称**：*Recombinant CDC37L1 expression and its role in cancer cell apoptosis*
**作者**：Lee S, et al.
**摘要**：利用大肠杆菌系统表达纯化CDC37L1重组蛋白，发现其通过抑制HSP90-EGFR相互作用降低癌细胞存活率，提示其作为肿瘤抑制蛋白的潜在机制。
3. **文献名称**：*Structural characterization of CDC37L1-HSP90 interaction using cryo-EM*
**作者**：Wang H, et al.
**摘要**：通过冷冻电镜解析重组CDC37L1与HSP90的复合物结构，揭示其结合界面与CDC37的差异，为设计靶向特定分子伴侣的药物提供依据。
---
**说明**：以上文献为假设性示例，实际研究中建议通过PubMed或Google Scholar以“CDC37L1 recombinant protein”或“CDC37L1 chaperone function”为关键词检索近期论文。真实研究多聚焦于CDC37L1与HSP90的互作机制、组织特异性蛋白折叠功能及疾病相关调控通路。
**Background of CDC37L1 Recombinant Protein**
CDC37L1 (Cell Division Cycle 37-like 1) is a member of the CDC37 family of molecular chaperones that plays a critical role in stabilizing and regulating client protein kinases. It functions as a co-chaperone for heat shock protein 90 (HSP90), aiding in the proper folding, maturation, and activation of kinase-dependent signaling pathways. Unlike its paralog CDC37. which predominantly supports oncogenic kinases (e.g., AKT, BRAF), CDC37L1 exhibits distinct substrate specificity and tissue expression patterns, suggesting specialized regulatory roles in cellular processes.
Structurally, CDC37L1 contains conserved domains for HSP90 interaction and kinase binding, enabling it to act as an adaptor between HSP90 and kinase clients. Studies highlight its involvement in stress response, cell cycle progression, and developmental signaling. Dysregulation of CDC37L1 has been linked to diseases such as cancer, where altered kinase activity drives tumorigenesis, and neurodegenerative disorders, reflecting its importance in maintaining proteostasis.
Recombinant CDC37L1 protein is engineered to study its biochemical functions, interactions, and therapeutic potential. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains chaperone activity and is used in *in vitro* assays to dissect kinase-HSP90 assembly mechanisms or screen for inhibitors targeting pathological kinase signaling. Its application extends to structural studies, aiding in the design of drugs that modulate chaperone-kinase networks.
Research on CDC37L1 continues to uncover its tissue-specific roles and differential client engagement compared to CDC37. emphasizing its unique contributions to cellular homeostasis and disease pathways.
×
