蛍光レポーター細胞株
VectorBuilderは、確実に安定した蛍光シグナルを持つ、様々なモノクローン由来レポーター細胞株を提供しています。蛍光イメージング、フローサイトメトリー、スクリーニングアッセイなど、幅広い研究アプリケーションに使用できます。
製品情報 プライスマッチ
出荷形態と保存方法
細胞（10% DMSO含有保存培地）はドライアイス便で輸送されます。受け取り後は、すぐに液体窒素の気相へ移してください（長期保存）。短期間（1週間以内）であれば-80°Cでの保存も可能です。
実験による検証
- EGFP発現 HT1080細胞
- EGFP発現 293T細胞
- EGFP/mCherry二重発現 293T細胞
図1. EGFP発現HT1080細胞の代表的な蛍光画像。倍率：100倍。
図2. EGFP発現293T細胞の代表的な蛍光画像。倍率：100倍。
図3. EGFPおよびmCherry発現293T細胞の代表的な蛍光画像。倍率：100倍。
リソース
FAQ
既製品安定細胞株は、混合クローン（プール）由来ですか、それともモノクローン由来ですか？
VectorBuilderの既製品安定細胞株はすべてモノクローン由来であり、一貫した再現性を保証します。当社のモノクローン由来細胞株は、厳格な品質管理（QC）と機能の検証を実施しており、応用アッセイに安心してご使用いただけます。
主な引用文献
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
主な使用製品:
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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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
主な使用製品:
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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