Abcam, ab204710, Flavin Adenine Dinucleotide (FAD) Assay Kit

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Flavin Adenine Dinucleotide (FAD) Assay Kit (ab204710) is an assay where FAD functions as the cofactor of an oxidase which catalyze the formation of a product that reacts with OxiRed probe generating color and fluorescence. Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Key facts
Detection method:Colorimetric/Fluorometric,
Sample types:Tissue Lysate, Plasma, Cell culture media, Serum, Cell Lysate,
Assay type:Enzyme activity,
Sensitivity:< 1 nmol/well,
Assay Platform:Microplate reader

Product details:
Flavin Adenine Dinucleotide (FAD) Assay Kit (ab204710) is an assay where FAD functions as the cofactor of an oxidase which catalyze the formation of a product that reacts with OxiRed probe generating color and fluorescence. FAD can be detected by either colorimetric (OD=570 nm) or fluorometric (Ex/Em=535/587 nm) methods. The kit provides a rapid, simple, ultra-sensitive, and reliable test suitable for high throughput assay of FAD. The lower limit of detection is less than 1 nM FAD.
FAD assay protocol summary
- add samples and standards to wells
- add reaction mix
- analyze with microplate reader until absorbance reaches 1.8 at 570 nm (or stop before then)
Other Notes
This product was previously called K357 Biovision FAD Colorimetric/Fluorometric Assay Kit. Biovision was acquired by Abcam in 2021.
Flavin Adenine Dinucleotide (FAD) is a redox cofactor which plays an important role in metabolism. FAD exists in different redox states and cycles between FAD, FADH and FADH2. The primary sources of reduced FAD in eukaryotic metabolism are the citric acid cycle and the beta oxidation reaction pathways.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Flavin Adenine Dinucleotide (FAD) sometimes referred to as flavins or FAD flavin is a coenzyme that plays a mechanical role by accepting and donating electrons in various biochemical reactions. It has a molecular mass of about 785.55 g/mol. FAD is widely expressed in cells particularly in the mitochondria where it participates in important redox reactions necessary for cellular energy production. The coenzyme is essential in processes that convert nutrients into energy facilitating cellular metabolism.
Biological function summary
FAD functions to transfer electrons in key metabolic reactions. It often operates as part of larger enzyme complexes like succinate dehydrogenase which is involved in the citric acid cycle and electron transport chain. In these complexes FAD acts as a redox-active cofactor cycling between its oxidized form (FAD) and its reduced form (FADH2 or FAD/FADH). This conversion is essential for maintaining the flow of electrons during cellular respiration enabling efficient ATP production.
Pathways
FAD is a critical component of the citric acid cycle and the electron transport chain two major metabolic pathways. In the citric acid cycle FADH2 is generated during the oxidation of succinate to fumarate aiding in the transfer of electrons to the electron transport chain. Along this pathway FAD interacts with proteins such as succinate dehydrogenase and other flavoproteins ensuring the efficient generation of ATP. These pathways highlight FAD's role in sustaining cellular respiration and energy homeostasis.
Disruptions in FAD-related enzymes can contribute to metabolic disorders like Multiple Acyl-CoA Dehydrogenase Deficiency (MADD) where FAD-linked enzyme deficiencies lead to impaired fatty acid oxidation. Additionally FAD's role in energy production implicates it in mitochondrial diseases with conditions such as Leigh syndrome arising from defects in FAD-dependent pathways and related proteins like succinate dehydrogenase. These associations highlight the importance of FAD as a cofactor in maintaining metabolic and mitochondrial health.