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Amino acids 40-493 form the expressed segment for recombinant Human MLYCD. The calculated molecular weight for this MLYCD protein is 55.9 kDa. This MLYCD protein is produced using e.coli expression system. The MLYCD gene fragment has been modified by fusing the N-terminal 10xHis tag and C-terminal Myc tag, providing convenience in detecting and purifying the recombinant MLYCD protein during the following stages.Human malonyl-CoA decarboxylase (MLYCD) is a mitochondrial enzyme that catalyzes the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide, playing a crucial role in fatty acid metabolism. By reducing malonyl-CoA levels, MLYCD alleviates its inhibitory effect on carnitine palmitoyltransferase 1 (CPT1), thus promoting fatty acid oxidation and mitochondrial energy production. MLYCD deficiency leads to the accumulation of malonyl-CoA, impairing fatty acid oxidation and causing symptoms such as cardiomyopathy, skeletal myopathy, and developmental delay. Research on MLYCD spans various areas, including lipid metabolism, mitochondrial function, and metabolic disorders, aiming to elucidate its role in health and disease and develop potential therapeutic strategies.
Amino acids 40-493 form the expressed segment for recombinant Human MLYCD. The calculated molecular weight for this MLYCD protein is 55.9 kDa. This MLYCD protein is produced using e.coli expression system. The MLYCD gene fragment has been modified by fusing the N-terminal 10xHis tag and C-terminal Myc tag, providing convenience in detecting and purifying the recombinant MLYCD protein during the following stages.Human malonyl-CoA decarboxylase (MLYCD) is a mitochondrial enzyme that catalyzes the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide, playing a crucial role in fatty acid metabolism. By reducing malonyl-CoA levels, MLYCD alleviates its inhibitory effect on carnitine palmitoyltransferase 1 (CPT1), thus promoting fatty acid oxidation and mitochondrial energy production. MLYCD deficiency leads to the accumulation of malonyl-CoA, impairing fatty acid oxidation and causing symptoms such as cardiomyopathy, skeletal myopathy, and developmental delay. Research on MLYCD spans various areas, including lipid metabolism, mitochondrial function, and metabolic disorders, aiming to elucidate its role in health and disease and develop potential therapeutic strategies.
| Cat.No | ACP02406 | Target Name | MLYCD |
|---|---|---|---|
| Target Synonyms | DCMC_HUMAN; hMCD; Malonyl CoA decarboxylase; Malonyl CoA decarboxylase mitochondrial; Malonyl coenzyme A decarboxylase; Malonyl-CoA decarboxylase; MCD; MGC59795; mitochondrial; Mlycd | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 40-493aa |
| Mol Weight | 55.9kDa | Protein Length | Full Length of Mature Protein |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | O95822 |
|---|
Uniprot Id
O95822
Target Species
Human
Target Name
MLYCD
Target Full Name
Malonyl-CoA decarboxylase, mitochondrial
Target Function
Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Target Involvement
Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)
Target Subcellular Location
Cytoplasm. Mitochondrion matrix. Peroxisome. Peroxisome matrix.
Target Tissue Specificity
Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.
Target Research Area
others
Target Synonyms
DCMC_HUMAN; hMCD; Malonyl CoA decarboxylase; Malonyl CoA decarboxylase mitochondrial; Malonyl coenzyme A decarboxylase; Malonyl-CoA decarboxylase; MCD; MGC59795; mitochondrial; Mlycd
Target Background
The product of this gene catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Malonyl-CoA is an intermediate in fatty acid biosynthesis, and also inhibits the transport of fatty acyl CoAs into mitochondria. Consequently, the encoded protein acts to increase the rate of fatty acid oxidation. It is found in mitochondria, peroxisomes, and the cytoplasm. Mutations in this gene result in malonyl-CoA decarboyxlase deficiency.
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