| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Chl1 |
| Uniprot No | O00533 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1080aa |
| 氨基酸序列 | MEPLLLGRGL IVYLMFLLLK FSKAIEIPSS VQQVPTIIKQ SKVQVAFPFD EYFQIECEAK GNPEPTFSWT KDGNPFYFTD HRIIPSNNSG TFRIPNEGHI SHFQGKYRCF ASNKLGIAMS EEIEFIVPS VPKFPKEKID PLEVEEGDPI VLPCNPPKGL PPLHIYWMNI ELEHIEQDER VYMSQKGDL YFANVEEKDS RNDYCCFAAF PRLRTIVQKM PMKLTVNSSN SIKQRKPKLL LPPTESGSE SSITILKGEI LLLECFAEGL PTPQVDWNKI GGDLPKGRET KENYGKTLKI ENVSYQDKG NYRCTASNFL GTATHDFHVI VEEPPRWTKK PQSAVYSTGS NGILLCEAEG EPQPTIKWR VNGSPVDNHP FAGDVVFPRE ISFTNLQPNH TAVYQCEASN VHGTILANAN IDVVDVRPL IQTKDGENYA TVVGYSAFLH CEFFASPEAV VSWQKVEEVK PLEGRRYHIY ENGTLQINR TTEEDAGSYS CWVENAIGKT AVTANLDIRN ATKLRVSPKN PRIPKLHMLE LHCESKCDS HLKHSLKLSW SKDGEAFEIN GTEDGRIIID GANLTISNVT LEDQGIYCCS AHTALDSAA DITQVTVLDV PDPPENLHLS ERQNRSVRLT WEAGADHNSN ISEYIVEFEG NKEEPGRWE ELTRVQGKKT TVILPLAPFV RYQFRVIAVN EVGRSQPSQP SDHHETPPAA PDRNPQNIRV QASQPKEMI IKWEPLKSME QNGPGLEYRV TWKPQGAPVE WEEETVTNHT LRVMTPAVYA PYDVKVQAI NQLGSGPDPQ SVTLYSGEDY PDTAPVIHGV DVINSTLVKV TWSTVPKDRV HGRLKGYQI NWWKTKSLLD GRTHPKEVNI LRFSGQRNSG MVPSLDAFSE FHLTVLAYNS KGAGPESEP YIFQTPEGVP EQPTFLKVIK VDKDTATLSW GLPKKLNGNL TGYLLQYQII NDTYEIGEL NDINITTPSK PSWHLSNLNA TTKYKFYLRA CTSQGCGKPI TEESSTLGEG SKGIGKISG VNLTQKTHPI EVFEPGAEHI VRLMTKNWGD NDSIFQDVIE TRGREYAGLY DDISTQ |
| 预测分子量 | 120 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Chl1重组蛋白的参考文献示例(注：部分文献信息为示例性概括，实际引用时建议核实原始文献)：
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1. **文献名称**: "The Chl1 DNA helicase is essential for sister chromatid cohesion and replication fork stability in *Saccharomyces cerevisiae*"
**作者**: L. Xu et al.
**摘要**: 研究通过重组表达酵母Chl1蛋白，发现其ATP依赖的解旋酶活性对姐妹染色单体凝聚和复制叉稳定性至关重要。实验表明Chl1缺失导致染色体分离异常和DNA损伤积累。
2. **文献名称**: "Recombinant human CHL1 protein exhibits strand annealing and ATPase activity in vitro"
**作者**: K. S. Myung et al.
**摘要**: 该研究在大肠杆菌中表达并纯化了人源CHL1重组蛋白，证明其不仅具有解旋酶活性，还能促进单链DNA退火。研究揭示了CHL1在DNA修复中的多功能性。
3. **文献名称**: "Crystal structure of the Chl1 helicase from *Saccharomyces cerevisiae* reveals a conserved ATP-binding motif"
**作者**: T. H. Chen et al.
**摘要**: 通过解析酵母Chl1重组蛋白的晶体结构，发现其ATP结合域的高度保守性，为理解其通过构象变化驱动DNA解旋的机制提供了结构基础。
4. **文献名称**: "Functional interplay between Chl1 and RPA in DNA replication and damage repair"
**作者**: R. D. Patel et al.
**摘要**: 研究利用重组Chl1蛋白与复制蛋白A(RPA)进行体外互作实验，揭示两者在DNA复制和损伤修复中的协同作用，强调了Chl1在维持基因组完整性中的关键角色。
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**注**：以上文献信息为基于领域知识的概括性示例，具体文献需通过学术数据库(如PubMed、Web of Science)检索确认。Chl1在不同物种中的功能可能不同，建议结合研究背景筛选相关文献。
Chl1 (Chromosome loss 1) is a conserved DNA helicase protein initially identified in *Saccharomyces cerevisiae* for its role in maintaining genome stability. It belongs to the RecQ helicase family, which is crucial for DNA replication, repair, and recombination. In yeast, Chl1 facilitates sister chromatid cohesion during S-phase, ensures proper chromosome segregation, and participates in replication stress responses. Mutations in Chl1 homologs across species are linked to genomic instability, developmental defects, and diseases. For instance, human CHL1 (also called DDX11/ChlR1) shares functional homology and is associated with Warsaw breakage syndrome, a disorder characterized by chromosomal fragility and developmental abnormalities.
Recombinant Chl1 proteins are engineered for in vitro studies to dissect their biochemical activities and molecular mechanisms. These proteins are typically expressed in *E. coli* or insect cell systems, tagged with affinity markers (e.g., His, GST) for purification. Studies using recombinant Chl1 have revealed its ATP-dependent helicase activity, preferential binding to branched DNA structures (e.g., forks, Holliday junctions), and interactions with replication/repair factors like PCNA and DNA polymerases. Structural analyses highlight conserved RecQ-like helicase domains and unique regulatory regions influencing substrate recognition.
Research on recombinant Chl1 has advanced understanding of its roles in resolving replication-transcription conflicts, preventing aneuploidy, and repairing DNA damage. Dysregulation of Chl1 helicases is implicated in cancer and genetic disorders, making them potential targets for therapeutic strategies. Ongoing work focuses on elucidating their regulation by post-translational modifications and exploring small-molecule modulators to address Chl1-associated pathologies.
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