MCAD Antibody (E-5): sc-365448

MCAD Antibody (E-5) is a mouse monoclonal IgG1 antibody that detects medium-chain acyl-CoA dehydrogenase (MCAD) in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-MCAD antibody (E-5) 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 in this enzyme can lead to severe metabolic disorders, including fasting hypoglycemia and hepatic dysfunction, particularly in infants. MCAD (E-5) monoclonal antibody recognizes a homotetramer composed of 421 amino acids, featuring mitochondrial protein transit peptides that facilitate its localization to the mitochondrion. Notably, the MCAD gene exhibits a high degree of sequence identity with its porcine counterpart, underscoring its evolutionary conservation and functional importance. MCAD (E-5) antibody enables researchers to gain insights into the metabolic pathways involving medium-chain fatty acids and the implications of MCAD deficiencies in human health.

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MCAD Antibody (E-5) References:

1. Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency.  |  Andresen, BS., et al. 2001. Am J Hum Genet. 68: 1408-18. PMID: 11349232
2. Molecular and functional characterisation of mild MCAD deficiency.  |  Zschocke, J., et al. 2001. Hum Genet. 108: 404-8. PMID: 11409868
3. Homozygosity for a severe novel medium-chain acyl-CoA dehydrogenase (MCAD) mutation IVS3-1G > C that leads to introduction of a premature termination codon by complete missplicing of the MCAD mRNA and is associated with phenotypic diversity ranging from sudden neonatal death to asymptomatic status.  |  Korman, SH., et al. 2004. Mol Genet Metab. 82: 121-9. PMID: 15171999
4. Oxidative stress induction by cis-4-decenoic acid: relevance for MCAD deficiency.  |  Schuck, PF., et al. 2007. Free Radic Res. 41: 1261-72. PMID: 17987455
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. Functional studies of 18 heterologously expressed medium-chain acyl-CoA dehydrogenase (MCAD) variants.  |  Koster, KL., et al. 2014. J Inherit Metab Dis. 37: 917-28. PMID: 24966162
7. 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
8. 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
9. Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: diagnosis by acylcarnitine analysis in blood.  |  Van Hove, JL., et al. 1993. Am J Hum Genet. 52: 958-66. PMID: 8488845
10. Rapid diagnosis of MCAD deficiency: quantitative analysis of octanoylcarnitine and other acylcarnitines in newborn blood spots by tandem mass spectrometry.  |  Chace, DH., et al. 1997. Clin Chem. 43: 2106-13. PMID: 9365395

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