Recombinant Rabbit monoclonal primary
ACADM Recombinant Rabbit Monoclonal Antibody [JE48-09] (ET7109-74)
Recombinant protein within human acadm aa 100-300.
Mouse liver tissue, Hela, SiHa, rat testis tissue, human liver cancer tissue, human kidney tissue, human esophagus tissue, mouse kidney tissue, mouse heart muscle tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein affinity purified.
ACAD 1 antibody; ACAD1 antibody; Acadm antibody; ACADM_HUMAN antibody; Acyl coenzyme A dehydrogenase antibody; Acyl coenzyme A dehydrogenase C 4 to C 12 straight chain antibody; FLJ18227 antibody; FLJ93013 antibody; FLJ99884 antibody; MCAD antibody; MCADH antibody; Medium chain acyl CoA dehydrogenase antibody; Medium chain fatty acyl CoA dehydrogenase antibody; Medium chain specific acyl CoA dehydrogenase antibody; Medium chain specific acyl CoA dehydrogenase mitochondrial antibody; Medium-chain specific acyl-CoA dehydrogenase antibody; mitochondrial antibody
Belongs to the acyl-CoA dehydrogenase family.
Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity (By similarity). These sites are deacetylated by SIRT3.
This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. Many of these mutations switch an amino acid building block in the ACADM enzyme. The most common amino acid substitution replaces lysine with glutamic acid at position 329 in the enzyme's chain of amino acids (also written as Lys329Glu or K329E). This mutation and other amino acid substitutions alter the enzyme's structure, reducing or abolishing its activity. Other mutations delete or duplicate part of the ACADM gene, which leads to an unstable enzyme that cannot function. Defects in this gene cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.