| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHD1L |
| Uniprot No | Q86WJ1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 704-897aa |
| 氨基酸序列 | SAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHAQSSSSSSRQLVP |
| 预测分子量 | 37.3 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CHD1L重组蛋白的3篇示例参考文献(基于研究领域常见主题构造，非真实文献)：
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1. **文献名称**: *Structural and Functional Analysis of CHD1L Recombinant Protein*
**作者**: Zhang, Y. et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了CHD1L重组蛋白，通过体外酶活实验证实其具有ATP依赖的染色质重塑活性，并解析了其与DNA结合的晶体结构，揭示了其C端结构域在底物识别中的关键作用。
2. **文献名称**: *CHD1L Recombinant Protein Promotes Hepatocellular Carcinoma Metastasis via Wnt/β-catenin Pathway*
**作者**: Li, X. et al.
**摘要**: 通过体外细胞实验发现，重组CHD1L蛋白的过表达可激活Wnt/β-catenin信号通路，促进肝癌细胞迁移和侵袭，提示其在肿瘤转移中的潜在分子机制。
3. **文献名称**: *CHD1L Recombinant Protein Facilitates DNA Repair by Interacting with PARP1*
**作者**: Wang, H. et al.
**摘要**: 利用重组CHD1L蛋白进行免疫共沉淀实验，发现其直接结合PARP1并增强其酶活性，在DNA损伤修复中发挥协同作用，为癌症治疗耐药性研究提供了新靶点。
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**注**：以上文献为示例，实际引用请通过PubMed、Google Scholar等平台检索真实发表论文。如需具体文献推荐，可提供更详细的研究方向。
CHD1L (Chromodomain Helicase DNA-Binding Protein 1-Like) is a member of the SNF2-like superfamily of chromatin-remodeling proteins, characterized by its conserved ATP-dependent helicase domain. It plays a critical role in DNA damage repair, replication, and transcriptional regulation. Initially identified as a gene amplified in hepatocellular carcinoma (HCC), CHD1L is frequently overexpressed in various cancers, including ovarian, colorectal, and breast cancers, where it promotes tumor progression by enhancing cell proliferation, metastasis, and chemoresistance. Its oncogenic activity is linked to multiple pathways, such as Wnt/β-catenin, PI3K/AKT, and epithelial-mesenchymal transition (EMT). CHD1L also interacts with PARP1 to facilitate DNA repair, contributing to genomic instability and therapeutic resistance.
Recombinant CHD1L protein, produced via heterologous expression systems (e.g., E. coli or mammalian cells), retains enzymatic and DNA-binding properties, enabling functional studies. It is widely used to investigate CHD1L’s biochemical mechanisms, including ATPase activity, chromatin remodeling, and protein-DNA interactions. Researchers employ it to screen inhibitors targeting its helicase domain or to validate binding partners in vitro. Additionally, recombinant CHD1L aids in structural studies (e.g., crystallography) to elucidate its molecular architecture and guide drug design. As a potential therapeutic target, understanding its role in carcinogenesis and DNA repair pathways highlights its relevance in developing precision oncology strategies. However, its pleiotropic functions in normal physiology, such as embryonic development and immune regulation, warrant cautious therapeutic targeting.
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