형광 리포터 Cell Lines
VectorBuilder는 강력하고 안정적인 형광 신호를 가진 다양한 단일 클론 유래 리포터 세포주를 제공하며, 형광 이미징, flow cytometry, 스크리닝 분석 등 광범위한 연구 응용분야에 사용 가능합니다.
주문 정보 Price Match
배송 및 보관
세포는 드라이아이스 (in 10% DMSO-containing culture medium)에 담겨 배송됩니다. 수령 즉시 장기 보관을 위해 cryovial을 액체질소 증기상 (Vapor Phase)에 옮겨 보관하십시오. 단기 보관 (1주일 이내)을 위해 -80°C에서 보관할 수도 있습니다.
실험에 의한 검증
- EGFP-expressing HT1080 cells
- EGFP-expressing 293T cells
- Dual-EGFP/mCherry-expressing 293T cells
Figure 1. EGFP를 발현하는 HT1080 세포의 형광 이미지. 배율: 100배.
Figure 2. EGFP를 발현하는 293T 세포의 형광 이미지. 배율: 100배.
Figure 3. EGFP와 mCherry를 발현하는 293T 세포의 형광 이미지. 배율: 100배.
정보 자료
자주 묻는 질문
Premade stable cell line은 mixed pools또는 single clone에서 유래한 것인가요?
VectorBuilder의 모든 Premade stable cell line은 일관성과 재현성을 보장하기 위해 단일 클론에서 유래합니다. VectorBuilder의 단일 클론 안정 세포주는 엄격한 품질관리 및 기능 검증을 거쳐 다운스트림 연구에 대한 확신을 제공합니다.
주요 인용 논문
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
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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
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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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