Application
ANS forms an inclusion complex with cyclodextrin. Such model systems are useful to mimic biological recognition and can be studied by measuring the change in fluorescence of free-ANS to complexed-ANS. When ANS enters the hydrophobic core of cyclodestrin, it’s fluorescence increases 1,2. Utilized in the reagent phase of a sodium-selective fiber-optic sensor. The reagent phase also contains a copper(II) polyelectrolyte, which binds to ANSA in the absence of sodium and quenches the fluorescence. In the presence of sodium, ANSA forms a cationic complex creating ion-pairs, causing it to fluoresce 3. ANS is often incorporated into di-block polymers and can be released by changes in the local environment (i.e., temperature, pH, etc.) 4,5,6. ANS is commonly used as a fluorescence probe to investigate molecular assemblies of surfactants and amphiphilic polymers because a blue shift of the emission maximum indicates the fluorophore is located in less polar media 7,8. Fluorescent probe for protein studies using methodologies such as steady-state and dynamic fluorescence measurements 9,10.
This product is an amphiphilic fluorescent probe for protein studies . Excitation of the unbound dye at 380 nm results in a low fluorescent emission with a maximum at 545 nm. The fluorescence intensity of ANS increases when the dye binds to the hydrophobic regions of a protein . The protein-ANS complex has an emission spectrum which is shifted to a broad maximum at 470 nm. At pH 8, protein causes a 40-fold increase in the relative quantum yield compared to free ANS in solution . ANS has been used to monitor protein conformational changes by binding to the hydrophobic regions of a protein , to gain new insight into protein binding interactions, often by acting as reporter or competitor ligands9,10, to investigate the visual excitation process and structural aspects of photoreceptor cell membranes , and to probe (and disrupt) the structure of both high- and low-density lipoproteins. It has also been used as a substrate in a chemiluminescent enzyme immunoassay system and as a dye for yeast viability determination. The conformational states for apo- and holo- yeast alcohol dehydrogenase were reported under conditions of low pH using ANS fluorescence . ANS is also commonly used as a fluorescence probe to investigate molecular assemblies of surfactants and amphiphilic polymers because a blue shift of its emission maximum indicates the probe is located in less polar environment 7 |
Application
ANS forms an inclusion complex with cyclodextrin. Such model systems are useful to mimic biological recognition and can be studied by measuring the change in fluorescence of free-ANS to complexed-ANS. When ANS enters the hydrophobic core of cyclodestrin, it’s fluorescence increases 1,2. Utilized in the reagent phase of a sodium-selective fiber-optic sensor. The reagent phase also contains a copper(II) polyelectrolyte, which binds to ANSA in the absence of sodium and quenches the fluorescence. In the presence of sodium, ANSA forms a cationic complex creating ion-pairs, causing it to fluoresce 3. ANS is often incorporated into di-block polymers and can be released by changes in the local environment (i.e., temperature, pH, etc.) 4,5,6. ANS is commonly used as a fluorescence probe to investigate molecular assemblies of surfactants and amphiphilic polymers because a blue shift of the emission maximum indicates the fluorophore is located in less polar media 7,8. Fluorescent probe for protein studies using methodologies such as steady-state and dynamic fluorescence measurements 9,10.
This product is an amphiphilic fluorescent probe for protein studies . Excitation of the unbound dye at 380 nm results in a low fluorescent emission with a maximum at 545 nm. The fluorescence intensity of ANS increases when the dye binds to the hydrophobic regions of a protein . The protein-ANS complex has an emission spectrum which is shifted to a broad maximum at 470 nm. At pH 8, protein causes a 40-fold increase in the relative quantum yield compared to free ANS in solution . ANS has been used to monitor protein conformational changes by binding to the hydrophobic regions of a protein , to gain new insight into protein binding interactions, often by acting as reporter or competitor ligands9,10, to investigate the visual excitation process and structural aspects of photoreceptor cell membranes , and to probe (and disrupt) the structure of both high- and low-density lipoproteins. It has also been used as a substrate in a chemiluminescent enzyme immunoassay system and as a dye for yeast viability determination. The conformational states for apo- and holo- yeast alcohol dehydrogenase were reported under conditions of low pH using ANS fluorescence . ANS is also commonly used as a fluorescence probe to investigate molecular assemblies of surfactants and amphiphilic polymers because a blue shift of its emission maximum indicates the probe is located in less polar environment 7 |