7298-65-9 Usage
Uses
Used in Research and Diagnostic Applications:
Fluorescein dibutyrate is used as a fluorogenic substrate for esterase and lipase to study the activity and function of these enzymes. Its fluorescence property allows for the easy detection and quantification of enzyme activity, making it a useful tool in research and diagnostic settings.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, fluorescein dibutyrate is used as a probe to evaluate the efficacy of drugs targeting esterase and lipase enzymes. By monitoring the fluorescence emitted upon enzyme hydrolysis, researchers can assess the potency and selectivity of drug candidates, aiding in the development of novel therapeutics.
Used in Environmental Monitoring:
Fluorescein dibutyrate can also be employed in environmental monitoring to detect the presence of esterase and lipase enzymes in various samples, such as soil, water, and air. This information can be used to assess the health of ecosystems and the potential impact of pollutants on enzyme activity.
Used in Analytical Chemistry:
In analytical chemistry, fluorescein dibutyrate serves as a sensitive and reliable indicator for the detection and quantification of esterase and lipase activity. Its use in high-throughput screening assays and other analytical techniques helps to streamline the process of enzyme analysis and improve the accuracy of results.
Check Digit Verification of cas no
The CAS Registry Mumber 7298-65-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,9 and 8 respectively; the second part has 2 digits, 6 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 7298-65:
(6*7)+(5*2)+(4*9)+(3*8)+(2*6)+(1*5)=129
129 % 10 = 9
So 7298-65-9 is a valid CAS Registry Number.
InChI:InChI=1/C28H24O7/c1-3-7-25(29)32-17-11-13-21-23(15-17)34-24-16-18(33-26(30)8-4-2)12-14-22(24)28(21)20-10-6-5-9-19(20)27(31)35-28/h5-6,9-16H,3-4,7-8H2,1-2H3
7298-65-9Relevant academic research and scientific papers
Cooperative hydrolysis of aryl esters on functionalized membrane surfaces and in micellar solutions
Poznik,Koenig
supporting information, p. 3175 - 3180 (2014/05/06)
Catalytic hydrolysis of peptides, proteins, phosphates or carboxylate esters in nature is catalysed by enzymes, which are efficient, fast and selective. Most of the hydrolytic chemical catalysts published so far mimic the active site of enzymes and contain metal complexes and amino acid residues. Their synthesis can be laborious, while the hydrolytic activity is still limited compared to enzymes. We present an approach that uses fluid membranes of vesicles and micelles as a support for amphiphilic additives, which cooperatively cleave aryl ester bonds. The membrane anchored bis-Zn(ii)-complex 1 is hydrolytically active and hydrolyses fluorescein diacetate (FDA) with a second order rate constant (k2) of 0.9 M-1 s-1. The hydrolytic activity is modulated by co-embedded membrane additives, bearing common amino acid side chain functional groups. With this approach, the hydrolytic activity of the system is enhanced up to 16 fold in comparison with cyclen 1 (k2 = 14.7 M-1 s-1). DOPC and DSPC lipids form at room temperature fluid or gel phase membranes, respectively. Omitting the lipid, micellar solutions were obtained with hydrolytic activity reaching k2 = 13.4 M-1 s-1. It is shown that cooperative hydrolysis is favoured in fluid membranes and micelles, allowing the active moieties to arrange freely. The embedding and dynamic self-assembly of membrane active components in fluid membranes and micelles provide facile access to hydrolytically active soft interfaces.
