Agarose gel reagent GFP-Trap

antibodyfor scientific researchprotein

Novel Antibody Fragment that binds GFP Fusion Proteins Analyze GFP fusion proteins – in a tube Fluorescent fusion proteins are popular tools to study protein localization and cellular dynamics. 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 jellyfish A. victoria are referred to as green fluorescent protein, or GFP. It’s easy to image cells using a GFP-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 GFP, and related fluorescent fusion proteins, for use in both cell biology studies and direct biochemical analysis. GFP-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.