Ad
related to: photoswitchable fluorescent proteinsbocsci.com has been visited by 10K+ users in the past month
Search results
Results from the WOW.Com Content Network
The first PAFP, Kaede (protein), was isolated from Trachyphyllia geoffroyi in a cDNA library screen designed to identify new fluorescent proteins. [1] A fluorescent green protein derived from this screen was serendipitously discovered to have sensitivity to ultraviolet light-- We happened to leave one of the protein aliquots on the laboratory ...
An animation of the structure of the dark state of dronpa protein Dronpa is a reversibly switchable photoactivatable fluorescent protein that is 2.5 times as bright as EGFP . [ 1 ] [ 2 ] Dronpa gets switched off by strong illumination with 488 nm (blue) light and this can be reversed by weak 405 nm UV light. [ 1 ]
While the use of fluorescent proteins was once limited to the green fluorescent protein , in recent years many other fluorescent proteins have been cloned. Unlike GFPs, which are derived from the luminescent jellyfish Aequorea victoria, fluorescent proteins derived from anthozoa, including Eos, emit fluorescence in the red spectral range.
Kaede is a photoactivatable fluorescent protein naturally originated from a stony coral, Trachyphyllia geoffroyi.Its name means "maple" in Japanese.With the irradiation of ultraviolet light (350–400 nm), Kaede undergoes irreversible photoconversion from green fluorescence to red fluorescence.
Photoactivatable fluorescent proteins change to longer emission wavelength upon illumination with UV light. In Kaede, this change is brought upon by cleavage of the chromophore tripeptide His62-Tyr63-Gly64. [5] This discovery paved the way for modern super resolution microscopy techniques like PALM or STORM. Retinylidene proteins, such as ...
S. cerevisiae septins revealed with fluorescent microscopy utilizing fluorescent labeling. In molecular biology and biotechnology, a fluorescent tag, also known as a fluorescent label or fluorescent probe, is a molecule that is attached chemically to aid in the detection of a biomolecule such as a protein, antibody, or amino acid.
The FAST-fluorogen reporting system is used to explore the living world, from protein reporting (e.g., for protein trafficking), protein-protein interaction monitoring (and a number of biosensors), to chemically induced dimerization. It is implemented in fluorescence microscopy, flow cytometry and any other fluorometric methods.
Multicolor imaging has been performed by using different activation wavelengths to distinguish dye-pairs, depending on the activator fluorophore used, [81] [82] [83] or using spectrally distinct photoswitchable fluorophores, either with or without activator fluorophores. [75] [84] [85] Photoswitchable fluorescent proteins can be used as well.
Ad
related to: photoswitchable fluorescent proteinsbocsci.com has been visited by 10K+ users in the past month