Inside bacterial cells, the green fluorescent protein (GFP) is typically encoded by a gene that can be introduced into the bacterial genome or expressed on a plasmid. The gene consists of coding sequences that allow the production of the GFP protein, which fluoresces green when exposed to specific wavelengths of light. The gene is regulated by bacterial promoters and terminators to control its expression level. The GFP protein is then synthesized within the bacterial cell and can be visualized using fluorescence microscopy or other techniques.
Go to http://www.tsienlab.ucsd.edu/Images.htm you will find bacterial colonies will and can express functional fluorescent proteins. As for the plasmid pQE30, it looks to fit into the category of expression at this level.
Organelles inside bacteria do not 'make' GFP. GFP can however be expressed in bacteria by adding the coding sequence for GFP to their genome. This can be done by using a plasmid virus containing the GFP gene sequence. When combined with the plasmid, a very small number of bacteria will take up the plasmid's genome into their own. These bacteria can be isolated by using the 'transform or die' mechanism. Bacteria that do not contain the plasmid are preferentially killed by adding an antibody to the agar. The normal bacteria will not be resistant to this, and will die, but the bacteria which have taken up the plasmid into their genome will also contain an antibody resistance gene. This allows them to live in the presence of the antibody. Since GFP was also added to these bacteria's genome, they will fluoresce.
The most common protein that is used as a 'tag' for other proteins is GFP. In order to do this, the GFP gene sequence is simply added at the end of the gene sequence for the target protein. GFP is particularly useful for this because it contains its own chromophore, and needs nothing else except the gene sequence to create its own light. This makes possible easy tracking of certain proteins without necessarily killing the tester animal.
The Nobel Prize in Chemistry 2008 was awarded jointly to Osamu Shimomura, Martin Chalfie and Roger Y. Tsien for the discovery and development of the green fluorescent protein, GFP.
No.
Aequorea GFP is a protein of 238 amino acids with a molecular weight of 27 or 30 kDa. Source: http://www.cryst.bbk.ac.uk/PPS2/projects/jonda/intro.htm
Yes, but it will not be green :)
Inside bacterial cells, the green fluorescent protein (GFP) is typically encoded by a gene that can be introduced into the bacterial genome or expressed on a plasmid. The gene consists of coding sequences that allow the production of the GFP protein, which fluoresces green when exposed to specific wavelengths of light. The gene is regulated by bacterial promoters and terminators to control its expression level. The GFP protein is then synthesized within the bacterial cell and can be visualized using fluorescence microscopy or other techniques.
Go to http://www.tsienlab.ucsd.edu/Images.htm you will find bacterial colonies will and can express functional fluorescent proteins. As for the plasmid pQE30, it looks to fit into the category of expression at this level.
Organelles inside bacteria do not 'make' GFP. GFP can however be expressed in bacteria by adding the coding sequence for GFP to their genome. This can be done by using a plasmid virus containing the GFP gene sequence. When combined with the plasmid, a very small number of bacteria will take up the plasmid's genome into their own. These bacteria can be isolated by using the 'transform or die' mechanism. Bacteria that do not contain the plasmid are preferentially killed by adding an antibody to the agar. The normal bacteria will not be resistant to this, and will die, but the bacteria which have taken up the plasmid into their genome will also contain an antibody resistance gene. This allows them to live in the presence of the antibody. Since GFP was also added to these bacteria's genome, they will fluoresce.
From punjabu rap
pGLO and GFP
The most common protein that is used as a 'tag' for other proteins is GFP. In order to do this, the GFP gene sequence is simply added at the end of the gene sequence for the target protein. GFP is particularly useful for this because it contains its own chromophore, and needs nothing else except the gene sequence to create its own light. This makes possible easy tracking of certain proteins without necessarily killing the tester animal.
He was a member of the (GFP) Geheime Feldpolizei. Secret field Police
this is awkward. defs not geometry mate. line refers to the "strain" of plant. try plant genetics??
Agrobacterium-mediated transformation using a plasmid containing a gene for GFP