GFP reporter (Aequorea victoria green-fluorescent protein) (Acc# AAA58246) is encoded in majority of our linearized baculovirus DNA vectors and recombinant baculoviruses. Their list is provided below. GFP allows monitoring of virus propagation, optimization of cultivation conditions, titration of virus stocks by "terminal green dilution", purification of GST-tagged proteins using GFP-Trap affinity reagents. For your convenience, we provide Green Control, which is a titrated reference stock of a baculovirus expressing GFP. GFP saves time and effort; there is no need for expensive baculovirus titration kits or specialized equipment. The only essential pieces required are the same 365 nm UV transilluminator and digital camera routinely used for ethidium bromide stained gels. Alternatively, you can determine virus titers by counting green foci of infected cells using fluorescent microscopy.
In addition, you can visualize GFP expressing cells by electron or light microscopy (Luby-Phelps et al., J. Histochem Cytochem. 51: 271-274, 2003), titer GFP-expressing vectors using flow cytometry (Hitt et al., Mol. Biotechnol., 14: 197-203, 2000), or use GFP to study the spread of nucleopolyhedrovirus infection in insects (Barrett et al., Tissue Cell, 30: 602-616, 1998).
Our pVL-GFP™ vector allows expression of target proteins in-fusion with GFP tag. The GFP tag is widely used for visualization and isolation of protein complexes, studies of protein-protein interactions, protein trafficking within the cells, and mechanisms of protein degradation (Cristea et al., Mol Cell Proteomics, 4:1933-41, 2005; Michaelson and Philips, Methods Enzymol, 406:296-315, 2006; Hayes et al., Cancer Lett., 206:129-35, 2004 ; Takeuchi et al., EMBO J., 26:123-31, 2007).
Especially useful is the ability of the GFP tag to misfold and loose its fluorescence if its fusion partner is misfolded. This property was used for selection of target protein mutants with improved solubility (Van den Berg et at, J Biotechnol, 121:291-8, 2006), for finding soluble proteins derived from randomly fragmented cDNAs (Nakayama and Ohara, Biochem Biophys Res Commun, 312:825-30, 2003), and in studies of protein aggregation (Schrodel and de Marco, BMC Biochem, 6:10, 2005).
Of particular interest are studies of GFP fusion aggregates with proteins related to protein folding diseases (Krobitsch and Lindquist, Proc Natl Acad Sci U S A, 97:1589-94, 2000; Wang et al., Hum Mol Genet., 14:3673-84, 2005; Pandey et al., Exp Neurol., 197:515-20, 2006; Jiang et al., J Biol Chem., 282:7912-20, 2007). Such fusions could be used for high throughput screening of compounds that inhibit aggregation of these important drug targets (Gazit, ASC Chemical Biology, 1:417-19, 2006). AB Vector offers some protein folding diseases targets in-fusion with GFP.
|Products equipped with GFP reporter|
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|Commercial use of GFP reporter requires licensing.|
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