Antibody RFP-Trap A

for biochemistrycell imagingprotein

These constructs usually fuse the entirety–or at least a functional domain–of a target protein to one of the many types of reporter fluorescent proteins. Those originally derived from the mushroom coral Discosoma sp. are commonly referred to as red fluorescent protein, or RFP. It’s easy to image cells using a RFP-fusion protein construct, though to get the full picture such imaging data is often combined with additional biochemical information for the protein (or protein domain) of interest. For such biochemical experiments, typically a second fusion protein is designed using a different “tag” domain that allows for purification. These additional in vitro analyses can be used to confirm functionality of the “tagged” fusion construct, as well as to pull out multi-protein complexes that may form in the cellular milieu. The lack of specific, reliable, and efficient reagents has limited the use of RFP, and related fluorescent fusion proteins, for use in both cell biology studies and direct biochemical analysis. RFP-Traps utilize super-high affinity alpaca antibody fragments coupled to agarose beads or magnetic agarose beads. These “Nanobody-Traps” are perfect for immuno-precipitation, immuno-purification, and immuno-pulldown experiments with up to 10-fold better purity (and yield) than that of conventional 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 RFP-fusions to be perfect candidates for immunoprecipitations, Co-IP, mass spectroscopy, enzyme activity measurements, and ChIP analysis.