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现货细胞稳转株

凭借我们在细胞工程领域的专业优势，云舟生物提供经过严格质量控制与效果验证的高质量现货细胞株，可确保其在多种应用场景下的可靠性和最佳效果，如CRISPR基因组编辑、荧光报告基因检测以及诱导型基因表达等。如需构建定制化的细胞稳转株，点击了解我们的细胞稳转株构建服务。

亮点
Reliability效果可靠
  • 来源于单克隆细胞株，确保实验的一致性与可重复性
  • 严格的质量控制，包括RT-qPCR和无菌/支原体检测
  • 经过功能验证，为下游实验提供可靠保障
Ready-to-use可直接使用
  • 简化您的工作流程，节省时间和精力
  • 可直接用于您的测试或基因递送实验
Fast_and_easy_ordering订购快速且便捷
  • 仅须几下点击即可选购您的细胞株
  • 几天内收到您的细胞株用于开展实验
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细胞稳转株产品
荧光报告基因细胞稳转株Fluorescent_Reporter_Cell_LinesCRISPR细胞稳转株CRISPR_Cell_LinesTet调控蛋白表达细胞稳转株Tet_Regulatory_Protein_Expression_Cell_Lines
精选文献
A lysine-rich cluster in the N-BAR domain of ARF GTPase-activating protein ASAP1 is necessary for binding and bundling actin filaments
Anjelika Gasilina, et al.
J Biol Chem, 2022, doi: 10.1016/j.jbc.2022.101700
使用的云舟生物产品或服务:
Abstract: Actin filament maintenance is critical for both normal cell homeostasis and events associated with malignant transformation. The ADP-ribosylation factor GTPase-activating protein ASAP1 regulates the dynamics of filamentous actin-based structures, including stress fibers, focal adhesions, and circular dorsal ruffles. Here, we have examined the molecular basis for ASAP1 association with actin. Using a combination of structural modeling, mutagenesis, and in vitro and cell-based assays, we identify a putative-binding interface between the N-Bin-Amphiphysin-Rvs (BAR) domain of ASAP1 and actin filaments. We found that neutralization of charges and charge reversal at positions 75, 76, and 79 of ASAP1 reduced the binding of ASAP1 BAR-pleckstrin homology tandem to actin filaments and abrogated actin bundle formation in vitro. In addition, overexpression of actin-binding defective ASAP1 BAR-pleckstrin homology [K75, K76, K79] mutants prevented cellular actin remodeling in U2OS cells. Exogenous expression of [K75E, K76E, K79E] mutant of full-length ASAP1 did not rescue the reduction of cellular actin fibers consequent to knockdown of endogenous ASAP1. Taken together, our results support the hypothesis that the lysine-rich cluster in the N-BAR domain of ASAP1 is important for regulating actin filament organization.
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Partial view-The KU-PARP14 axis differentially regulates DNA resection at stalled replication forks by MRE11 and EXO1
The KU-PARP14 axis differentially regulates DNA resection at stalled replication forks by MRE11 and EXO1
Ashna Dhoonmoon, Claudia M. Nicolae & George-Lucian Moldovan.
Nature Communications, 2022, doi: 10.1038/s41467-022-32756-5
使用的云舟生物产品或服务:
Abstract: Suppression of nascent DNA degradation has emerged as an essential role of the BRCA pathway in genome protection.In BRCA-deficient cells, the MRE11 nuclease is responsible for both resection of reversed replication forks, and accumulation of single stranded DNA gaps behind forks. Here, we show that the mono-ADP-ribosyltransferase PARP14 is a critical co-factor of MRE11. PARP14 is recruited to nascent DNA upon replication stress in BRCA-deficient cells, and through its catalytic activity, mediates the engagement of MRE11. Loss or inhibition of PARP14 suppresses MRE11-mediated fork degradation and gap accumulation, and promotes genome stability and chemoresistance of BRCA-deficient cells. Moreover, we show that the KU complex binds reversed forks and protects them against EXO1-catalyzed degradation. KU recruits the PARP14-MRE11 complex, which initiates partial resection to release KU and allow long-range resection by EXO1. Our work identifies a multistep process of nascent DNA processing at stalled replication forks in BRCA-deficient cells.
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常见问题解答

所有现货细胞稳转株是来源于多克隆细胞群还是单克隆细胞株？ ▼

云舟生物提供的所有现货细胞稳转株均来源于单克隆细胞株，以保证实验的一致性和可重复性。我们的单克隆细胞株经过严格的QC以及功能验证，可为您的下游应用提供充分的保障。

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