rGFP
Description
rGFP is purified by proprietary chromatographic techniques.
Product Specs
HYQQNTPIGD GPVLLPDNHY LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYK.
Product Science Overview
The discovery of GFP dates back to the 1960s when Osamu Shimomura first purified the protein from Aequorea victoria . Shimomura’s work laid the foundation for further research, and in 1992, Douglas Prasher successfully cloned the GFP gene . This breakthrough allowed Martin Chalfie’s lab to express GFP in Escherichia coli and Caenorhabditis elegans, demonstrating its potential as a marker for gene expression . Roger Tsien’s lab later improved GFP’s fluorescence and stability, making it a widely used research tool . For their contributions, Shimomura, Chalfie, and Tsien were awarded the Nobel Prize in Chemistry in 2008 .
GFP consists of 238 amino acids and has a molecular mass of approximately 27 kDa . The protein’s structure includes a chromophore, which is responsible for its fluorescence. The chromophore forms spontaneously within the protein without the need for additional cofactors or enzymes . GFP has a major excitation peak at 395 nm and a minor one at 475 nm, with an emission peak at 509 nm, which falls within the green portion of the visible spectrum .
Recombinant GFP refers to GFP that has been genetically engineered and produced using recombinant DNA technology. This involves inserting the GFP gene into a plasmid vector, which is then introduced into a host organism, such as bacteria, yeast, or mammalian cells . The host organism expresses the GFP gene, producing the fluorescent protein. Recombinant GFP can be fused to other proteins of interest, allowing researchers to study protein localization, interactions, and expression patterns within living cells .
GFP has revolutionized biological research by providing a non-invasive method to visualize and track proteins in real-time. Some key applications include:
- Reporter Gene: GFP is commonly used as a reporter gene to monitor gene expression and regulation. By fusing the GFP gene to a promoter of interest, researchers can observe the spatial and temporal patterns of gene expression .
- Protein Localization: GFP fusion proteins enable the study of protein localization within cells. By tagging a protein of interest with GFP, researchers can track its movement and distribution in living cells .
- Protein-Protein Interactions: Split-GFP technology allows the detection of protein-protein interactions. This involves splitting the GFP molecule into two non-fluorescent fragments, which fluoresce when brought together by interacting proteins .
- Biosensors: GFP-based biosensors have been developed to detect various cellular processes, such as changes in pH, ion concentrations, and enzyme activities .
