GFP Produits

The introduction of green fluorescent protein (GFP) in the 1990s has allowed us to look into living, developing embryos, and see how cells form tissues and how organ morphogenesis proceeds in real time.¹ The original green fluorescent protein (GFP) was discovered back in the early 1960s when researchers studying the bioluminescent properties of the Aequorea victoria jellyfish isolated a blue-light-emitting bioluminescent protein called aequorin together with another protein that was eventually named the green-fluorescent protein. Aequorin and GFP work together in the light organs of A. victoria to convert Ca²⁺-induced luminescent signals into the green luminescence that is characteristic of the species. After GFP was cloned, it was first used for tracking gene expression in bacteria and the sensory neurons of the nematode C. elegans. There are many techniques to utilize GFP in a live cell imaging experiment. The most direct way of utilizing GFP is to directly attach it to a protein of interest. Our GFP Catcher (ABIN5311508) is the ideal tool for effective pulldown of GFP-fusion proteins. The GFP-Catcher is based on a high-affinity single-domain antibody (sdAb) that is covalently immobilized on 4% cross-linked agarose beads. It is highly specific to GFP and its derivatives like EGFP, mEGFP, or tSapphire and suitable for immunoprecipitation (IP) and related applications like Co-IP, ChIP and RIP. ² (1) Affolter, M., Seeing is Believing, or How GFP Changed My Approach to Science, PMID: 26970610 DOI: 10.1016/bs.ctdb.2015.12.001. (2) Gert-Jan Kremers, Sarah G. Gilbert, Paula J. Cranfill, et al. Fluorescent proteins at a glance. J Cell Sci. 2011 Jan 15; 124(2): 157–160. Published online 2010 Dec 27. doi: 10.1242/jcs.072744.