Platform Reagent

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Transfected Cell Culture (TCC)
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Purpose For fast and convenient characterization of interactions between GFP- and RFP-tagged proteins in live mammalian cells by conventional fluorescence microscopy.
Brand F2H®
Characteristics transfection supplement enabling assembly of the nuclear PPI-platform

Intracellular analysis of protein-protein interactions (PPIs) is crucial for understanding of intimate relationships of proteins within their native cellular environment. Besides, cell-based analysis is often required to support biochemical data obtained with in vitro PPI assays.
With the Fluorescent Two-Hybrid (F2H®) Kit, evaluation of selected PPIs can be rapidly carried out in live mammalian cells. Interactions are visualized by simple fluorescence microscopy as co-localization of green- and red fluorescent signals at a PPI-platform in the nucleus of F2H®-Cells, transiently co-transfected with interacting GFP- and RFP-tagged proteins.

Restrictions For Research Use only
Concentration 1 mg/mL
Storage 4 °C/-20 °C
Storage Comment Store Platform Reagent at +4°C (short term) or in -20°C (long term).
Expiry Date 6 months
Supplier Images
 image for Platform Reagent (ABIN1889497) F2H® principle: - F2H cells (BHK origen) carry a GFP-anchoring platform in the nucleu...
 image for Platform Reagent (ABIN1889497) F2H® result: Exemplary F2H images obtained by fluorescence microscopy
Left, inte...
 image for Platform Reagent (ABIN1889497) An overview image of co-transfected F2H®-Cells at 20X magnification. Cells were PFA-f...
 image for Platform Reagent (ABIN1889497) F2H®-Cells were co-transfected with interacting proteins, fixed, stained with a nucle...
Product cited in: Yurlova, Derks, Buchfellner, Hickson, Janssen, Morrison, Stansfield, Brown, Ghadessy, Lane, Rothbauer, Zolghadr, Krausz: "The fluorescent two-hybrid assay to screen for protein-protein interaction inhibitors in live cells: targeting the interaction of p53 with Mdm2 and Mdm4." in: Journal of biomolecular screening, Vol. 19, Issue 4, pp. 516-25, 2014 (PubMed).

Wolf, Mantri, Heim, Müller, Fichter, Mackeen, Schermelleh, Dadie, Leonhardt, Vénien-Bryan, Kessler, Schofield, Böttger: "The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization." in: The Biochemical journal, Vol. 453, Issue 3, pp. 357-70, 2013 (PubMed).

Brown, Quah, Jong, Goh, Chiam, Khoo, Choong, Lee, Yurlova, Zolghadr, Joseph, Verma, Lane: "Stapled peptides with improved potency and specificity that activate p53." in: ACS chemical biology, Vol. 8, Issue 3, pp. 506-12, 2013 (PubMed).

Wei, Joseph, Sim, Yurlova, Zolghadr, Lane, Verma, Ghadessy: "In vitro selection of mutant HDM2 resistant to Nutlin inhibition." in: PLoS ONE, Vol. 8, Issue 4, pp. e62564, 2013 (PubMed).

Mortusewicz, Fouquerel, Amé, Leonhardt, Schreiber: "PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms." in: Nucleic acids research, Vol. 39, Issue 12, pp. 5045-56, 2011 (PubMed).