MCD Protein, Human (His)

MCD proteins catalyze the conversion of malonyl-CoA to acetyl-CoA, ensuring that only methylmalonyl-CoA serves as a substrate for fatty acid synthase, producing fatty acids with multiple methyl side chains. MCD Protein, Human (His) is the recombinant human-derived MCD protein, expressed by E. coli , with N-6*His labeled tag. The total length of MCD Protein, Human (His) is 452 a.a., .

The MCD protein plays a pivotal role in cellular metabolism by catalyzing the conversion of malonyl-CoA to acetyl-CoA. Particularly significant in fatty acid biosynthesis, MCD selectively eliminates malonyl-CoA, ensuring that methyl-malonyl-CoA becomes the exclusive substrate for fatty acid synthase. This selective removal mechanism contributes to the production of fatty acids with multiple methyl side chains. In peroxisomes, MCD is implicated in the degradation of intraperoxisomal malonyl-CoA, a byproduct of peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Beyond its involvement in lipid metabolism, MCD influences the metabolic balance between glucose and lipid oxidation in muscle, independent of insulin signaling alterations. Additionally, MCD may play a role in mitigating ischemic injury by promoting glucose oxidation, highlighting its multifaceted impact on cellular functions and metabolic pathways.

Human

E. coli

N-6*His

O95822 (M40-S491)

23417

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.