V5-Trap Magnetic Particles M-270

Analyze V5 fusion proteins in a tube
The V5-tag is a popular, well-established peptide tag used by many laboratories. With the V5-Trap, 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 V5-Traps success are the use of super-high affinity Camelidae antibody fragments called Nanobodies. V5-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.

V5-Trap for immunoprecipitations
Immunoprecipitations (IP) of V5-tagged protein extracts of V5-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.

M-270 particles are made for the largest fusion proteins and large protein complexes! 
GFP-Trap Magnetic Particles M-270 are specifically designed to capture fusion proteins that are too big for our standard GFP-Trap Agarose or Magnetic Agarose beads. The larger and more consistently-sized M-270 provide plenty of room for loads of large GFP-fusion protein to bind on their surface.  Just as fast and clean as the other GFP-Trap reagents — This version maintains a simple one-step isolation of your GFP fusion protein and its interacting factors, so your lab sacrifices nothing.

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.