Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 3
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-FLAD1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
FLAD1 also known as FAD synthase is an enzyme that plays a role mechanically in the synthesis of Flavin Adenine Dinucleotide (FAD) from ATP and FMN (Flavin Mononucleotide). FLAD1 has an approximate mass of 66 kDa. It is expressed in a variety of tissues with high levels in liver heart and kidneys. Its primary responsibility is to ensure the sufficient production of FAD necessary for various metabolic enzymes and biological processes.
Biological function summary
FLAD1 facilitates essential cellular processes by enabling the synthesis of FAD a cofactors required for the functioning of oxidoreductase enzymes involved in redox reactions. FAD forms part of several enzyme complexes vital for energy production and cellular respiration including those complexes located within the mitochondria. FLAD1's action allows cells to maintain metabolic activities such as the Krebs cycle and the electron transport chain.
Pathways
Flavin Adenine Dinucleotide produced by FLAD1 is fundamental for proper mitochondrial function through participation in the oxidative phosphorylation and the beta-oxidation pathways. These pathways are critical for efficient ATP production. Related proteins that also contribute to these pathways include succinate dehydrogenase and acyl-CoA dehydrogenase which depend on FAD to perform their metabolic roles.
Disruptions in FLAD1 function can contribute to metabolic-related conditions. The dysfunctional production of FAD can associate with mitochondrial disorders where energy production is impaired and FLAD1 mutations are linked to conditions like multiple acyl-CoA dehydrogenase deficiency (MADD). Proteins such as ETFDH another enzyme involved in the electron transport chain have connections with FLAD1 especially in these metabolic disorders highlighting the enzyme's importance in maintaining normal cellular function.
