Adenosine 5′-diphosphate-2′,3′-dialdehyde (oADP) is used to stimulate the permeability transition in mitochondria. oADP and oATP modify the duration and intensity of firefly luciferase-containing reactions. oADP has been used as an affinity label for the NAD+ binding site of recombinant Candida boidinii formate dehydrogenase (FDH) and to inactivate muscle pyruvate kinase.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Listings
Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.
Archives of biochemistry and biophysics, 314(2), 261-267 (1994-11-01)
Addition of periodate-oxidized ATP (oATP) to firefly luciferase-containing reaction mixtures enhanced light production when the reaction mixture contained > approximately 8 microM ATP. The time course of light production was changed from a flash pattern to a constant light output
The British journal of nutrition, 120(5), 557-566 (2018-07-31)
This study examines the associations between maternal Traditional dietary pattern adherence and HIV/treatment with neonatal size and adiposity in urban, black South Africans, as well as how specific maternal factors - that is BMI and gestational weight gain (GWG) -
Biochimica et biophysica acta, 1363(3), 209-216 (1998-04-29)
Periodate-oxidized ADP (oADP)2 and periodate-oxidized ATP (oATP) stimulate the permeability transition in energized rat liver mitochondria measured as the Ca2+-efflux induced by Ca2+ and Pi. In the presence of Mg2+ and Pi, mitochondria lose intramitochondrial adenine nucleotides at a slow
European journal of biochemistry, 267(22), 6657-6664 (2000-10-29)
The 2',3'-dialdehyde derivative of ADP (oADP) has been shown to be an affinity label for the NAD+ binding site of recombinant Candida boidinii formate dehydrogenase (FDH). Inactivation of FDH by oADP at pH 7.6 followed biphasic pseudo first-order saturation kinetics.
Archives of biochemistry and biophysics, 253(1), 133-137 (1987-02-15)
Rabbit muscle pyruvate kinase was inactivated by 2', 3'-dialdehyde ADP with the incorporation of one molecule of reagent per enzyme subunit. The inactivated protein was digested with trypsin after reduction and carboxymethylation. The labeled peptide was isolated by gel filtration
Questions
Reviews
★★★★★ No rating value
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.