mNeonGreen-Trap Affinity Reagents

Analyze mNeonGreen fusion proteins in a tube

As imaging technology advances, many researchers have turned toward super resolution imaging platforms. Common fluorophores, such as GFP, may not always be the best fit for this application. mNeonGreen is an ultra-bright monomeric yellow-green fluorescent proteins derived from the lancelet, Branchiostoma lanceolatum. mNeonGreen fusions are a great choice for use in fluorescence, confocal & super resolution microscopy. With the mNeonGreen-Trap, specific for this non-GFP variant, yields of fusion proteins purification are high and free from heavy and light-chain contaminants, all in under 30 minutes. Save time, save effort and get cleaner results.

The secret to mNeonGreen-Traps success are the use of super-high affinity Camelidae antibody fragments called Nanobodies. mNeonGreen-Traps may be used for immuno-precipitation, immuno-purification and immuno-pull down experiments with up to 10-fold better purity and yield than that of classic mouse monoclonal antibodies. Compatible with a variety of source materials, Nanobody-Traps may be used with mammalian cells, tissues & organs, bacteria, yeast and even plants. These reagents allow your mNeonGreen-fusions to be perfect candidates for immunoprecipitations, Co-IP, mass spectroscopy, and enzyme activity measurements.

mNeonGreen-Trap for immunoprecipitations

Immunoprecipitations (IP) of mNeonGreen from protein extracts of mNeonGreen-expressing E.coli cells.  Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western Blotting. Unlike conventional antibodies, the mNeonGreen-Trap is free from heavy and/or light chain contaminants and therefore yields cleaner results.

Camelidae single-domain antibodies are like IgGs on steroids

The family of animals known as Camelidae (camels, llamas, and alpacas) produce functional antibodies devoid of light chains, so-called "heavy chain" antibodies. These heavy chain antibodies recognize and bind their antigens via a single variable domain. When cleaved from their carboxy tail, these barrel-shaped structures (2x3 nm) are extraordinarily small, naturally-occurring, and intact antigen binding fragments (MW of 13 kDa). These fragments, called Nanobodies, are characterized by high specificity, affinities in the low nanomolar range, and dissociation constants in the sub-nanomolar range (typically 10- to 100-fold better than mouse IgGs). The compact size of Nanobodies makes them extremely stable at temperatures up to 70°C, and functional even in 2M NaCl or 0.5% SDS. These small and powerful antibody fragments can be used in a variety of unique applications. They will open up your research possibilities.