MCAD Antibody (G-4): sc-365109

MCAD Antibody (G-4) is a mouse monoclonal IgG1 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). Anti-MCAD antibody (G-4) plays a crucial role in identifying the presence and levels of MCAD, a key enzyme involved in the mitochondrial fatty acid β-oxidation pathway, which is essential for the metabolism of medium-chain fatty acids ranging from C4 to C12. The proper functioning of MCAD is vital, as deficiencies can lead to severe metabolic disorders, including fasting hypoglycemia and hepatic dysfunction, particularly in infants. MCAD (G-4) monoclonal antibody recognizes a homotetramer composed of 421 amino acids, featuring mitochondrial protein transit peptides that facilitate localization to the mitochondrion, where MCAD catalyzes the initial reaction in the β-oxidation process. Notably, MCAD exhibits a high degree of sequence identity with its porcine counterpart, underscoring evolutionary conservation and importance in energy metabolism. Anti-MCAD antibody (G-4) enables researchers to gain insights into the metabolic pathways involving medium-chain fatty acids and their implications in various physiological and pathological conditions.

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MCAD Antibody (G-4) References:

1. A successful strategy for preimplantation diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency.  |  Ioulianos, A., et al. 2000. Prenat Diagn. 20: 593-8. PMID: 10913960
2. Molecular and functional characterisation of mild MCAD deficiency.  |  Zschocke, J., et al. 2001. Hum Genet. 108: 404-8. PMID: 11409868
3. Binding of the human 'electron transferring flavoprotein' (ETF) to the medium chain acyl-CoA dehydrogenase (MCAD) involves an arginine and histidine residue.  |  Parker, AR. 2003. J Enzyme Inhib Med Chem. 18: 453-62. PMID: 14692513
4. Specific diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in dried blood spots by a polymerase chain reaction (PCR) assay detecting a point-mutation (G985) in the MCAD gene.  |  Gregersen, N., et al. 1991. Clin Chim Acta. 203: 23-34. PMID: 1769118
5. Detection of urinary hexanoylglycine in the diagnosis of MCAD deficiency from newborn screening.  |  Downing, M., et al. 2008. J Inherit Metab Dis. 31: 550. PMID: 18649007
6. Mutation screening of the medium-chain acyl-CoA dehydrogenase (MCAD) and the ornithine transcarbamylase (OTC) genes by multiplex PCR amplification and sequencing.  |  Horn, MP., et al. 2009. Clin Chem Lab Med. 47: 56-9. PMID: 19055470
7. Facile and restricted pathways for the dissociation of octenoyl-CoA from the medium-chain fatty acyl-CoA dehydrogenase (MCAD)-FADH2-octenoyl-CoA charge-transfer complex: energetics and mechanism of suppression of the enzyme's oxidase activity.  |  Kumar, NR. and Srivastava, DK. 1995. Biochemistry. 34: 9434-43. PMID: 7626613
8. Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD). Demonstration of impaired transfer of K304E-variant MCAD from its complex with hsp60 to the native tetramer.  |  Saijo, T., et al. 1994. J Biol Chem. 269: 4401-8. PMID: 7905878
9. Characterization of wild-type human medium-chain acyl-CoA dehydrogenase (MCAD) and mutant enzymes present in MCAD-deficient patients by two-dimensional gel electrophoresis: evidence for post-translational modification of the enzyme.  |  Bross, P., et al. 1994. Biochem Med Metab Biol. 52: 36-44. PMID: 7917465
10. Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation.  |  Bross, P., et al. 1993. Biochim Biophys Acta. 1182: 264-74. PMID: 8104486

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