MCAD Antibody (A-4): sc-365030

MCAD Antibody (A-4) is a mouse monoclonal IgG2b antibody that detects medium-chain acyl-CoA dehydrogenase (MCAD) in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). MCAD plays a crucial role in the mitochondrial fatty acid β-oxidation pathway, specifically catalyzing the initial reaction in the breakdown of medium-chain acyl-CoAs ranging from C4 to C12. This enzymatic function is vital for energy production, particularly during periods of fasting when the body relies on fat stores for fuel. Deficiencies in MCAD can lead to severe metabolic disorders, including fasting hypoglycemia and hepatic dysfunction, which can be life-threatening, especially in infants. MCAD is a homotetramer composed of 421 amino acids and features mitochondrial protein transit peptides, ensuring proper localization within the mitochondria. Notably, MCAD exhibits 88% sequence identity with its porcine counterpart, highlighting evolutionary conservation and importance across species. Anti-MCAD antibody (A-4) is an essential tool for researchers studying metabolic pathways and related disorders.

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MCAD Antibody (A-4) References:

1. Adult presentation of MCAD deficiency revealed by coma and severe arrythmias.  |  Feillet, F., et al. 2003. Intensive Care Med. 29: 1594-7. PMID: 12897989
2. Pulmonary haemorrhage and cardiac dysfunction in a neonate with medium-chain acyl-CoA dehydrogenase (MCAD) deficiency.  |  Maclean, K., et al. 2005. Acta Paediatr. 94: 114-6. PMID: 15858970
3. Seemingly neutral polymorphic variants may confer immunity to splicing-inactivating mutations: a synonymous SNP in exon 5 of MCAD protects from deleterious mutations in a flanking exonic splicing enhancer.  |  Nielsen, KB., et al. 2007. Am J Hum Genet. 80: 416-32. PMID: 17273963
4. Medium-chain fatty acids accumulating in MCAD deficiency elicit lipid and protein oxidative damage and decrease non-enzymatic antioxidant defenses in rat brain.  |  Schuck, PF., et al. 2009. Neurochem Int. 54: 519-25. PMID: 19428797
5. MCAD mutations identified in newborn screening cause different levels of enzymatic dysfunction.  |  Ehrnhoefer, DE. 2009. Clin Genet. 76: 146-8. PMID: 19673949
6. A Large Intragenic Deletion in the ACADM Gene Can Cause MCAD Deficiency but is not Detected on Routine Sequencing.  |  Searle, C., et al. 2013. JIMD Rep. 11: 13-6. PMID: 23546811
7. Investigation of beta-oxidation intermediates in normal and MCAD-deficient human fibroblasts using tandem mass spectrometry.  |  Nada, MA., et al. 1995. Biochem Mol Med. 54: 59-66. PMID: 7551818
8. Molecular genetic characterization and urinary excretion pattern of metabolites in two families with MCAD deficiency due to compound heterozygosity with a 13 base pair insertion in one allele.  |  Gregersen, N., et al. 1994. J Inherit Metab Dis. 17: 169-84. PMID: 7967471
9. A rare disease-associated mutation in the medium-chain acyl-CoA dehydrogenase (MCAD) gene changes a conserved arginine, previously shown to be functionally essential in short-chain acyl-CoA dehydrogenase (SCAD).  |  Andresen, BS., et al. 1993. Am J Hum Genet. 53: 730-9. PMID: 8102510
10. A silent A to G mutation in exon 11 of the medium-chain acyl-CoA dehydrogenase (MCAD) gene.  |  Andresen, BS., et al. 1993. Hum Mol Genet. 2: 488. PMID: 8504313

The preferred MCAD antibody is MCAD Antibody (E-8): sc-271931.