Anti-MVD Antibody Picoband® Fluoro594 Conjugated

The enzyme mevalonate pyrophosphate decarboxylase (MVD; EC 4.1.1.33) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate. This unusual enzyme decarboxylates and dehydrates its substrate while hydrolyzing ATP. As a unique enzyme in one of the early steps in cholesterol biosynthesis, MVD may be a useful target for drugs aimed at lowering serum cholesterol levels. This gene is mapped to chromosome 16q24.3 based on an alignment of the MVDsequence.

A synthetic peptide corresponding to a sequence at the N-terminus of human MVD, which shares 97.3% amino acid (aa) sequence identity with both mouse and rat MVD.

Cancer, Cancer Metabolism, Cardiovascular, Cholesterol Metabolism, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism of Lipids and Lipoproteins, Pathways and Processes, Signal Transduction

1. Luan, J., Niu, Z., Zhang, J., Crosby, M. E., Zhang, Z., Chu, X., Wang, Z., Huang, W., Xiang, L., Zheng, Z. A novel locus for disseminated superficial actinic porokeratosis maps to chromosome 16q24.1-24.3. Hum. Genet. 129: 329-334, 2011. 2. Toth, M. J., Huwyler, L. Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J. Biol. Chem. 271: 7895-7898, 1996. 3. Zhang, Z., Li, C., Wu, F., Ma, R., Luan, J., Yang, F., Liu, W., Wang, L., Zhang, S., Liu, Y., Gu, J., Hua, W., and 13 others. Genomic variations of the mevalonate pathway in porokeratosis.eLife 4: e06322, 2015. Note: Electronic Article. Erratum: eLife 5: e14383, 2016.