A Reversibly Photodissociable Split GFP

Creation of a caspase-3 sensing system using a combination of split-GFP and split-intein.

A genetically encodable caspase-3 sensing system has been created using self-assembling split-GFP, in which a C-terminal fragment is "covalently" cyclized via a caspase-3 substrate sequence mediated by split-intein. The specific cleavage of the cyclic C-terminal fragment by caspase-3 induces the GFP reassembly and fluorescence recovery.

Supporting Information for: Light Activated Reassembly of Split GFP

Specific cell surface labeling of GPCRs using split GFP

Specific cell surface labeling is essential for visualizing the internalization processes of G-protein coupled receptors (GPCRs) and for gaining mechanistic insight of GPCR functions. Here we present a rapid, specific, and versatile labeling scheme for GPCRs at living-cell membrane with the use of a split green fluorescent protein (GFP). Demonstrated with two GPCRs, GPR17 and CysLT2R, we show t...

Fluorescent Labeling of Antibody Fragments Using Split GFP

Antibody fragments are easily isolated from in vitro selection systems, such as phage and yeast display. Lacking the Fc portion of the antibody, they are usually labeled using small peptide tags recognized by antibodies. In this paper we present an efficient method to fluorescently label single chain Fvs (scFvs) using the split green fluorescent protein (GFP) system. A 13 amino acid tag, derive...

Generation of a dual-functional split-reporter protein for monitoring membrane fusion using self-associating split GFP.

Split reporter proteins capable of self-association and reactivation have applications in biomedical research, but designing these proteins, especially the selection of appropriate split points, has been somewhat arbitrary. We describe a new methodology to facilitate generating split proteins using split GFP as a self-association module. We first inserted the entire GFP module at one of several...