Green fluorescent protein

Question: Would the GFP gene in a pGLO transformed E. coli be activated by a sugar other than arabinose? Introduction: Green Fluorescent Protein, produced by the bioluminescent jellyfish Aequorea victoria, is a protein that fluoresces green under ultraviolet light. Since its discovery, properties of the protein have been improved by mutations in the gene resulting in the expansion of its spectrum, which now contains brighter variants and multiple different colors. GFP is used in a wide variety

1. Green Fluorescent Protein (GFP) GFP is a widely used tool in the field of Molecular biology and Cell biology. It involves emission of fluorescence under Ultra Violet light which allows for direct investigation into the inner working of cells. Green Fluorescent Protein was first isolated from the jelly fish Aequorea victoria by Osamu Shimomura (Shimomura et al., 1962). Since its discovery, it has become useful in the field of science. The GFP chromophore is formed from tri peptide in the primary

scientists. This species of jellyfish produces green bioluminescence from small photo organs located on its umbrella. In the 1960, while working at Princeton University, the scientist Osamu Shimomura was attempting to answer the question how some organisms can produce light which led him to work on the jellyfish and the discovery of GFP. In his work with the jellyfish Aequorea Victoria, he discovered and isolated Aequorin, the bioluminescence protein.

In the 1960's, Green Fluorescent Protein was discovered to be responsible for Aequorea victoria's fluorescence under UV light (Niwa et al., 1996). Today, GFP is often used in protein tagging and has made it possible for scientists to study expression and track proteins in vivo. With the rising importance of GFP fusion proteins and other recombinant vectors, the metal affinity of Histidine helps to make the protein purification process easier (Lilius et al., 1991). His tags are commonly used to

Title: Purification of Green Fluorescent Protein Introduction: Transformation is used to introduce a gene coding for a foreign protein into bacteria. Hydrophobic Interaction Chromatography (HIC) is used to purify the foreign protein. Protein gel electrophoresis is used to check and analyze the pure protein. Research scientists use Green Fluorescent Protein (GFP) as a master or tag to learn about the biology of individual cells and multicultural organisms. This lab introduces a rapid method

allows scientists to follow with their own eyes the dynamic movements of specific proteins as they occur within the living cell is the green fluorescent protein. This is a protein that is extracted from only a few jellyfish. This diffuses a green fluorescent colored light. The green fluorescent protein can be blended to the protein and can work normally and so does the protein itself that it is binded to. The protein is not affected and can be moved and transported throughout the cell and can then

Abstract section Green fluorescent protein (GFP) comes from the jellyfish Aequorea Victoria is rare proteins with high fluoresce and absorbance. The purpose this experiments is to purify and express a His2-tagged recombinant from of GFP (rGFP) from the E. coli strain BL21(DE3)< pRSETA-GFPUV > through a series of experiments by using Ni+2 agarose affinity chromatography technology. The GFPuv gene (UV-optimized GFP) was over expressed in the E. Coil strain BL21 (DE3) (pLysS) as an n-terminal His6/Xpress

naturally competent can be tested with an artificial transformation, such as what we will use in this experiment. Methods used can obtain things such as chemical mutagens or radiation (1). The gene used for the transfer is the GFP gene (Green Fluorescent Protein), which gives an illuminating appearance under a UV light when conducted properly,

Purpose: Green fluorescent protein (gfp) and blue fluorescent protein (bfp) extracted from bacteria were separated by chromatography by means of a molecular sieve matrix. This process utilized the proteins size and shape and was able to separate it from the other molecules and be collected in test tubes. The tubes containing the desired protein will glow under U.V. light. By running an electrophoresis gel with these proteins, one can compare the protein bands and be able to determine the approximate

contains the ability to fluoresce green under ultraviolet light because of the Green Fluorescent Protein (GFP). pGLO also encompasses an antibiotic resistance gene, bla, that allows E. coli to grow in media that contains penicillin derivative antibiotics such as ampicillin. We conclude that the protein, GFP, is indeed responsible for the green fluorescence as pGLO contains the gene to encode for it, which is turned on when arabinose is present. Additionally, when the protein is subjected to denaturation