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Chromotek offers GFP Nanobodies conjugated to beads for immunoprecipitation and unconjugated GFP Nanobodies/VHHs:GFP-Trap Agarose: anti-GFP Nanobody conjugated to agarose beadsGFP-Trap Magnetic Agarose: anti-GFP Nanobody conjugated to magnetic agarose beadsGFP-Trap Magnetic Particles M-270: anti-GFP Nanobody conjugated to magnetic particles M-270 for analysis of very large proteins/complexes.

Endogenous proteins do not contain protein or peptide tags and therefore are sometimes difficult to detect in an assay. One solution that enables easy detection is to genetically fuse protein and peptide tags to the protein of interest. Tagged proteins can be used for purposes such as immunoprecipitation, microscopy, protein purification, Western blotting, protein arrays, etc. Proteins fused to GFP are called GFP-tagged proteins or GFP-fusion proteins. GFP-tagged proteins are often used for fluorescence microscopy, immunoprecipitation, protein purification, and Western blotting.

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GFP is a protein and, like other proteins, it can be expressed by living organisms. Once GFP is expressed and properly folded, it shows fluorescent properties. If excited by light in the ultra-violet or blue spectrum, GFP emits green light (for more details please see sections 8 and 9). This property has had an enormous impact on cell biology: GFP and proteins fused to GFP can be detected as GFP works as a fluorescent tag. This has actually made lots of new experiments possible.4. What are GFP-tagged proteins and GFP-fusion proteins.

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GFP is an endogenous protein from the jellyfish Aequorea Victoria. It was isolated by Osamu Shimomura in 1962. In 1992, the sequence of GFP was cloned (Douglas Prasher) and Martin Chalfie’s lab expressed the sequence in vivo. Roger Tsien’s lab improved GFP and managed to convert it into a commonly used research tool. In 2008, The Nobel Prize in Chemistry was awarded “for the discovery and development of the green fluorescent protein, GFP.” See Roger Tsien’s Nobel Prize lecture here.

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The two-ring chromophore of GFP absorbs and emits light, e.g., light photons, in the visible green spectrum.The chromophore, actually a two-ring chromophore, of GFP lies in the center of a beta-barrel structure. The two-ring chromophore is formed by oxidation and cyclization of the backbone of 3 amino acids: Threonine 65, Tyrosine 66, and Glycine 67. This process occurs during the folding of the protein and depends on different factors such as pH, temperature, and oxygen concentration.

Can GFP antibodies detect YFP, CFP, or other derivatives?That depends on the antibody. Most GFP antibodies also recognize other derivatives, especially if there are just a few amino acid substitutions compared to GFP or EGFP. For example, the GFP-Trap recognizes AcGFP, Clover, eGFP, Emerald, GFP, GFP5, GFP Envy, GFP, S65T, mGFP, mPhluorin, PA-GFP, Superfolder GFP, TagGFP, TagGFP2, monomeric eGFP K206A, CFP, YFP, Citrine, eCitrine, eYFP, Venus, Ypet, BFP (click here for a complete list).Is GFP still fluorescent after fixation?There is no general answer to this question as it depends on the fixation method and procedure.

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GFP stands for green fluorescent protein. GFP is a fluorescent protein that can be expressed in vivo. If GFP is exposed to light, it emits a green fluorescent signal. This property has had an enormous impact on cell biology by enabling the imaging of almost any protein, in transcription studies by working as a reporter gene, and in biochemical applications.

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Nano-Trap system provides fast, reliable, and effective immunoprecipitation of fusion proteins. More than 3,000 peer-reviewed articles have already been published using ChromoTek's Nano-Traps.

Left: beta-barrel structure and fluorescent core of enhanced GFP (EGFP), a GFP derivate; right: magnification of the fluorescent core, the two-ring chromophore

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GFP and GFP derivate EGFP have a β-barrel structure. In the center of this β-barrel, there are 3 amino acids. These acids and the cyclization and oxidation of their backbone form a two-ring chromophore.

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Many fluorescent proteins are based on the GFP sequence. These fluorescent proteins are genetically engineered and have different properties such as different excitation/emission spectra, photo or pH-stability, folding properties, half-time etc. Here is a rough overview: