Résultats pour gfp green fluorescent protein

gfp green fluorescent protein
GFP Green Fluorescent Protein goat antibody.
It is extensively used in laboratory as a reporter molecule to label and study cellular and subcellular proteins in living cells using a wide range of applications. Antibodies to GFP protein are used in immunoblotting and ELISA. GFP protein has molecular weight of 27 kDa. Related products: GFP Green Fluorescent Protein monoclonal.
Benchmarking Various Green Fluorescent Protein Variants in Bacillus subtilis, Streptococcus pneumoniae, and Lactococcus lactis for Live Cell Imaging Applied and Environmental Microbiology.
The use of Aequorea victoria green fluorescent protein GFP and its derivatives has tremendously increased our knowledge of bacterial cell biology 1, 2. Because of the possibilities to examine protein localization or gene expression in live cells, new improved variants of GFP appear regularly.
Green Fluorescent Protein GFP: Applications, Structure, and Related Photophysical Behavior Chemical Reviews.
Journal of Chemical Theory and Computation 2018, 14 4, 2117-2126. Yi-Hui Chen, Robert Sung, Kuangsen Sung. Synthesis and Properties of the p-Sulfonamide Analogue of the Green Fluorescent Protein GFP Chromophore: The Mimic of GFP Chromophore with Very Strong NH Photoacid Strength.
GFP Green Fluorescent Protein Bringing Light to Life Antibody News: Novus Biologicals.
Home GFP Green Fluorescent Protein Bringing Light to Life. GFP Green Fluorescent Protein Bringing Light to Life. Fri, 05/17/2013 1040.: GFP green florescent protein, originally discovered in the jellyfish Aequorea victoria, 1 is one of the most extensively investigated and exploited proteins in the area of life sciences.
Expression of Green Fluorescent Protein in the Retina of KnockIn GFPRhodopsin Fusion Mice IOVS ARVO Journals.
Sign In or Create an Account. Young; Expression of Green Fluorescent Protein in the Retina of KnockIn GFPRhodopsin Fusion Mice. Download citation file.: ARVO 1962-2015; The Authors 2016-present. Abstract: Purpose: Rhodopsingreen fluorescent protein GFP fusion rhogfp mice have their native rhodopsin gene replaced by the human rhodopsin gene with its C terminus modified to encode an enhanced GFP fusion.
Green Fluorescent Protein Proteopedia, life in 3D.
11.0 11.1 11.2 11.3 11.4 11.5 6 Cubitt, AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien R. Understanding, improving, and using green fluorescent protein. Trends in Biochemical Sciences. Bublitz G, King BA, Boxer SG. Electronic structure of the chromophore in green fluorescent protein GFP.
Green fluorescent protein is lighting up fungal biology. USGS Publications Warehouse. Lock.
Download citation as: RIS Dublin Core. Prasher 42 cloned a cDNA for the green fluorescent protein GFP gene from the jellyfish Aequorea victoria in 1992. Shortly thereafter, to the amazement of many investigators, this gene or derivatives thereof were successfully expressed and conferred fluorescence to bacteria and Caenorhabditis elegans cells in culture 10, 31, followed by yeast 24, 39, mammals 40, Drosophila 66, Dictyostelium 23, 30, plants 28, 49, and filamentous fungi 54.
Fluorescent Proteins 101: Green Fluorescent Protein GFP.
Y145A and H148D. Stabilizes the structure of Cerulean derivatives. F99S, M153T, V163A. Improves folding at 37C, reduces aggregation at high concentrations. Red-shifts the wavelength yellow derivatives. Interferes with dimer interface monomeric derivatives. K26R, Q80R, N146H, H231L, and probably others. A multitude of applications. Due to its size and ease of use, GFP and other fluorescent proteins have become a mainstay in molecular biology. Scientists can easily utilize GFP-containing plasmids as a means to many functional ends. Weve listed our favorites below, but many other uses currently exist, and new GFP technology is constantly being developed! Fusion tagging: One of the most common uses, GFP can be fused to the N or C-terminus of a protein, which allows the scientist to visualize when and where the gene is expressed.
Green fluorescent protein: A perspective.
The topics discussed are primarily those in which my research group has made a contribution and include structure and function of the GFP polypeptide, the mechanism of fluorescence emission, excited state protein transfer, the design of ratiometric fluorescent protein biosensors and an overview of the fluorescent proteins derived from coral reef animals.

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