既製品安定細胞株
VectorBuilderは、細胞株エンジニアリングの専門知識を活かし、厳格な品質管理と検証を経た高品質でそのまま使用可能な細胞株を提供しています。作製済みの安定発現細胞株により、CRISPRゲノム編集、蛍光レポーターアッセイ、誘導性遺伝子発現などのアプリケーションにおいて、信頼できる成果を上げることが可能となります。カスタム安定細胞株作製については、VectorBuilderの安定発現細胞株作製サービスをご参照ください。
特長
信頼性
- モノクローン由来細胞株で、一貫性と再現性を保証
- RT-qPCRや無菌性・マイコプラズマ検査を含む厳格な品質管理（QC）
- 機能検証済みのため、実験に使用する際に安心
Ready-to-Use
- ワークフローを簡素化し、時間と労力を節約
- アッセイや遺伝子導入実験をすぐに開始可能
迅速かつ簡単な注文
- 数クリックで細胞株を選択
- すぐに実験に使用できる細胞を輸送日数＋数日で受け取り
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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