The ACAD10 Polyclonal Antibody (PACO07541) is a vital tool for researchers studying the ACAD10 protein, which plays a key role in fatty acid metabolism. This antibody, produced in rabbits, exhibits high specificity for human samples and has been extensively validated for Western blot applications. By binding to the ACAD10 protein, this antibody allows for accurate detection and analysis in a variety of cell types, making it a valuable asset for studies in metabolism, lipid biology, and mitochondrial function.
ACAD10 is an essential enzyme involved in fatty acid oxidation, a process critical for energy production and metabolic homeostasis. Dysregulation of ACAD10 has been linked to metabolic disorders, including fatty liver disease and insulin resistance, highlighting its importance in maintaining metabolic health. Researchers investigating these conditions can use this antibody to explore the role of ACAD10 in disease pathology and potential therapeutic interventions targeting fatty acid metabolism.
acyl-Coenzyme A dehydrogenase family, member 10;ACAD10;MGC5601 ;
UniProt Protein Function:
ACAD10: Acyl-CoA dehydrogenase only active with R- and S-2- methyl-C15-CoA. Belongs to the acyl-CoA dehydrogenase family. 4 isoforms of the human protein are produced by alternative splicing.Protein type: EC 1.3.99.-; Mitochondrial; OxidoreductaseChromosomal Location of Human Ortholog: 12q24.12Cellular Component: mitochondrionMolecular Function: acyl-CoA dehydrogenase activity; FAD binding; hydrolase activity; transferase activity, transferring phosphorus-containing groups
UniProt Protein Details:
NCBI Summary:
This gene encodes a member of the acyl-CoA dehydrogenase family of enzymes (ACADs), which participate in the beta-oxidation of fatty acids in mitochondria. The encoded enzyme contains a hydrolase domain at the N-terminal portion, a serine/threonine protein kinase catlytic domain in the central region, and a conserved ACAD domain at the C-terminus. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Nov 2008]
