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AB204710

Flavin Adenine Dinucleotide (FAD) Assay Kit

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(16 Publications)

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.
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Functional Studies - Flavin Adenine Dinucleotide (FAD) Assay Kit (AB204710)
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Supplier Data

Functional Studies - Flavin Adenine Dinucleotide (FAD) Assay Kit (AB204710)

Typical FAD Standard Curve (Colorimetric Assay).

Functional Studies - Flavin Adenine Dinucleotide (FAD) Assay Kit (AB204710)
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Supplier Data

Functional Studies - Flavin Adenine Dinucleotide (FAD) Assay Kit (AB204710)

Typical FAD Standard Curve (Fluorometric Assay).

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

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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.

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What's included?

{ "values": { "100Test": { "sellingSize": "100 Test", "publicAssetCode":"ab204710-100Test", "assetComponentDetails": [ { "size":"1 x 1.2 mL", "name":"Stop Solution II", "number":"AB204710-CMP05", "productcode":"" }, { "size":"1 x 0.2 mL", "name":"OxiRed™ Probe", "number":"AB204710-CMP04", "productcode":"AB309437" }, { "size":"1 x 1 Vial", "name":"FAD Standard", "number":"AB204710-CMP03", "productcode":"" }, { "size":"1 x 1 Vial", "name":"FAD Enzyme Mix", "number":"AB204710-CMP02", "productcode":"" }, { "size":"1 x 25 mL", "name":"FAD Assay Buffer", "number":"AB204710-CMP01", "productcode":"" } ] } } }
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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
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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.
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Product protocols

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Target data

See full target information Flavin adenine dinucleotide
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Publications (16)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 15:6525 PubMed39988719

2025

Lysine-specific demethylase 1 (LSD1) suppresses cellular senescence by riboflavin uptake-dependent demethylation activity.

Applications

Unspecified application

Species

Unspecified reactive species

Taiichi Osumi,Taiki Nagano,Tetsushi Iwasaki,Jotaro Nakanishi,Kazuyuki Miyazawa,Shinji Kamada

Nature communications 16:212 PubMed39747079

2025

Mitochondrial-cytochrome c oxidase II promotes glutaminolysis to sustain tumor cell survival upon glucose deprivation.

Applications

Unspecified application

Species

Unspecified reactive species

Yong Yi,Guoqiang Wang,Wenhua Zhang,Shuhan Yu,Junjie Fei,Tingting An,Jianqiao Yi,Fengtian Li,Ting Huang,Jian Yang,Mengmeng Niu,Yang Wang,Chuan Xu,Zhi-Xiong Jim Xiao

Redox biology 78:103413 PubMed39536592

2024

Riboflavin kinase binds and activates inducible nitric oxide synthase to reprogram macrophage polarization.

Applications

Unspecified application

Species

Unspecified reactive species

Xiao Shan,Zemin Ji,Baochen Wang,Yanan Zhang,Hongyuan Dong,Weijia Jing,Yanzhao Zhou,Penghui Hu,Yan Cui,Zihan Li,Sujun Yu,Jinxue Zhou,Ting Wang,Long Shen,Yuping Liu,Qiujing Yu

Nature communications 15:6587 PubMed39097623

2024

Targeting fatty acid oxidation enhances response to HER2-targeted therapy.

Applications

Unspecified application

Species

Unspecified reactive species

Ipshita Nandi,Linjia Ji,Harvey W Smith,Daina Avizonis,Vasilios Papavasiliou,Cynthia Lavoie,Alain Pacis,Sherif Attalla,Virginie Sanguin-Gendreau,William J Muller

The EMBO journal 43:2636-2660 PubMed38778156

2024

The immune response to RNA suppresses nucleic acid synthesis by limiting ribose 5-phosphate.

Applications

Unspecified application

Species

Unspecified reactive species

Pushpak Bhattacharjee,Die Wang,Dovile Anderson,Joshua N Buckler,Eveline de Geus,Feng Yan,Galina Polekhina,Ralf Schittenhelm,Darren J Creek,Lawrence D Harris,Anthony J Sadler

Nature communications 15:3563 PubMed38670969

2024

LSD1 inhibition circumvents glucocorticoid-induced muscle wasting of male mice.

Applications

Unspecified application

Species

Unspecified reactive species

Qingshuang Cai,Rajesh Sahu,Vanessa Ueberschlag-Pitiot,Sirine Souali-Crespo,Céline Charvet,Ilyes Silem,Félicie Cottard,Tao Ye,Fatima Taleb,Eric Metzger,Roland Schuele,Isabelle M L Billas,Gilles Laverny,Daniel Metzger,Delphine Duteil

Cell stem cell 31:570-581.e7 PubMed38521057

2024

Autofluorescence is a biomarker of neural stem cell activation state.

Applications

Unspecified application

Species

Unspecified reactive species

Christopher S Morrow,Kelsey Tweed,Sabina Farhadova,Alex J Walsh,Bo P Lear,Avtar Roopra,Ryan D Risgaard,Payton C Klosa,Zachary P Arndt,Ella R Peterson,Michelle M Chi,Allison G Harris,Melissa C Skala,Darcie L Moore

iScience 27:109276 PubMed38450153

2024

Chronic stress alters hepatic metabolism and thermodynamic respiratory efficiency affecting epigenetics in C57BL/6 mice.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandra Nikolic,Pia Fahlbusch,Nele-Kathrien Riffelmann,Natalie Wahlers,Sylvia Jacob,Sonja Hartwig,Ulrike Kettel,Martina Schiller,Matthias Dille,Hadi Al-Hasani,Jörg Kotzka,Birgit Knebel

Journal of medicinal chemistry 66:5774-5801 PubMed37027002

2023

Acetyl-Click Screening Platform Identifies Small-Molecule Inhibitors of Histone Acetyltransferase 1 (HAT1).

Applications

Unspecified application

Species

Unspecified reactive species

Jitender D Gaddameedi,Tristan Chou,Benjamin S Geller,Amithvikram Rangarajan,Tarun A Swaminathan,Danielle Dixon,Katherine Long,Caiden J Golder,Van A Vuong,Selene Banuelos,Robert Greenhouse,Michael P Snyder,Andrew M Lipchik,Joshua J Gruber

Molecular biology of the cell 32:br10 PubMed34524871

2021

Riboflavin transporter SLC52A1, a target of p53, suppresses cellular senescence by activating mitochondrial complex II.

Applications

Unspecified application

Species

Unspecified reactive species

Taiki Nagano,Yuto Awai,Shione Kuwaba,Taiichi Osumi,Kentaro Mio,Tetsushi Iwasaki,Shinji Kamada
View all publications
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