200940-00-7

Upstream product

• 74-89-5 methylamine 
• 52507-17-2 (Z)-4-((2-methyl-5-oxooxazol-4(5H)-ylidene)methyl)phenyl acetate 
• 71428-89-2 N-crotonylglycine 
• 108-24-7 acetic anhydride 
• 123-08-0 4-hydroxy-benzaldehyde 
• 124-40-3 dimethyl amine 
• 123-75-1 pyrrolidine 
• 67-56-1 methanol 
• 123-11-5 4-methoxy-benzaldehyde 
• 98081-75-5 2-azido-3-(4-methoxyphenyl)acrylic acid methyl ester 
• 101820-96-6 (Z)-5-(4-methoxybenzylidene)-2,3-dimethyl-3,5-dihydro-4H-imidazol-4-one 
• 878-00-2 4-formylphenyl acetate 

Relevant academic research and scientific papers

Red-Shifted Substrates for FAST Fluorogen-Activating Protein Based on the GFP-Like Chromophores

A genetically encoded fluorescent tag for live cell microscopy is presented. This tag is composed of previously published fluorogen-activating protein FAST and a novel fluorogenic derivative of green fluorescent protein (GFP)-like chromophore with red fluorescence. The reversible binding of the novel fluorogen and FAST is accompanied by three orders of magnitude increase in red fluorescence (580–650 nm). The proposed dye instantly stains target cellular proteins fused with FAST, washes out in a minute timescale, and exhibits higher photostability of the fluorescence signal in confocal and widefield microscopy, in contrast with previously published fluorogen:FAST complexes.

Facile synthesis, characterisation and anti-inflammatory activities of ferrocenyl ester derivatives of 4-arylidene-5-imidazolinones

This article describes the synthesis, optoelectronic properties and anti-inflammatory activities of a series of seven ferrocenyl ester-linked 4-arylidene-5-imidazolinone conjugates. Three different types of ortho-, meta- and para-substituted ferrocenyl es

A synthetic approach to GFP chromophore analogs from 3-azidocinnamates. Role of methyl rotors in chromophore photophysics

We have suggested a novel combinatorial approach for synthesis of otherwise inaccessible GFP chromophore analogs, and studied the influence of aliphatic substituents on their pH-dependent spectral properties. We found that the demethylation at C or N posi

Isomerization in fluorescent protein chromophores involves addition/elimination

The green fluorescent protein (GFP) chromophore undergoes both photochemical and thermal isomerizations. Typically, the Z form is more stable and undergoes photochemical conversion to the E form followed by thermal reversion over a period of seconds or minutes. Although the mechanism of the thermal reversion has been the subject of some investigations, the surprisingly low activation energy for this process has not sparked any controversy. We now show that the chromophore is surprisingly stable in both E and Z forms and that the facile thermal reversion is the result of a novel nucleophilic addition/elimination mechanism. This observation may have implications for the intervention of such processes, as well as blinking and kindling, in fluorescent proteins. Copyright

Synthesis of alaninyl and N-(2-aminoethyl)glycinyl amino acid derivatives containing the green fluorescent protein chromophore in their side chains for incorporation into peptides and peptide nucleic acids

Artificial amino acids carrying either the chromophore of the Green Fluorescent Protein (GFP) or a modification as their side chains have been synthesized: Boc-protected alaninyl derivatives and Fmoc-protected N-(2-aminoethyl)glycine-functionalized amino

Synthesis and spectroscopic studies of model red fluorescent protein chromophores.

[reaction: see text]. Here we describe the synthesis and spectroscopic characterization of two compounds designed to model the chromophore in DsRed, a red fluorescent protein. Comparison with model green fluorescent protein (GFP) chromophores indicates th

Fluorescent properties of model chromophores of tyrosine-66 substituted mutants of Aequorea green fluorescent protein (GFP)

In an ethanol-glass marix at 77 K, model compounds of the chromophores of recombinant GFP-Y66F, GFP-Y66W, and GFP-Y66H exhibited fluorescence properties close to those of the corresponding mutant proteins.

Mechanism of the redox reaction of the aequorea green fluorescent protein (GFP)

A model compound, 4-(4-hydroxypheny])methylideneimidazol-5 undergoes a reversible redox reaction identical to that of the Aequorea green fluorescent protein (GFP), strongly suggesting that the GFP chromophore is derived via the autoxidation of a nonfluorescent dihydro precursor in dihydro-GFP.