MUT Antibody (D-1): sc-390978

MUT Antibody (D-1) is a mouse monoclonal IgG1 kappa light chain antibody that detects MUT protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). Anti-MUT antibody (D-1) is available as the non-conjugated form. MUT protein, also known as methylmalonyl Coenzyme A mutase, is a crucial 750 amino acid mitochondrial matrix protein that functions as a homodimer and is a member of the methylmalonyl-CoA mutase family. MUT protein plays a vital role in the metabolism of various amino acids, odd-chain fatty acids, and cholesterol through involvement in the degradation pathway via propionyl-CoA during the tricarboxylic acid cycle, a key metabolic process that provides energy and building blocks for cellular functions. MUT protein is induced by adenosylcobalamin, also known as coenzyme B12 or vitamin B12, which is essential for enzymatic activity. Mutations in the gene encoding MUT protein, located on human chromosome 6, lead to methylmalonic aciduria type mut (MMAM), a serious metabolic disorder characterized by symptoms such as lethargy, vomiting, failure to thrive, hypotonia, neurological deficits, and early mortality. There are two forms of MMAM: mut(o), which shows no detectable enzymatic activity, and mut(−), which retains some residual cobalamin-dependent activity, highlighting the critical nature of MUT protein in human health and metabolism.

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MUT Antibody (D-1) References:

1. Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria.  |  Crane, AM., et al. 1992. J Clin Invest. 89: 385-91. PMID: 1346616
2. Three novel and six common mutations in 11 patients with methylmalonic acidemia.  |  Kobayashi, A., et al. 2006. Pediatr Int. 48: 1-4. PMID: 16490061
3. Differential diagnosis of mut and cbl methylmalonic aciduria by DNA-mediated gene transfer in primary fibroblasts.  |  Wilkemeyer, MF., et al. 1991. J Clin Invest. 87: 915-8. PMID: 1671869
4. Gene induction for the treatment of methylmalonic aciduria.  |  Hu, R., et al. 2009. J Gene Med. 11: 361-9. PMID: 19199343
5. Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia.  |  Crane, AM. and Ledley, FD. 1994. Am J Hum Genet. 55: 42-50. PMID: 7912889
6. Glutathione deficiency as a complication of methylmalonic acidemia: response to high doses of ascorbate.  |  Treacy, E., et al. 1996. J Pediatr. 129: 445-8. PMID: 8804337
7. Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations.  |  Ledley, FD. and Rosenblatt, DS. 1997. Hum Mutat. 9: 1-6. PMID: 8990001
8. Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation.  |  Janata, J., et al. 1997. Hum Mol Genet. 6: 1457-64. PMID: 9285782
9. Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12.  |  Mücher, G., et al. 1998. Genomics. 48: 40-5. PMID: 9503014