Anti-GALE Antibody Picoband® Fluoro488 Conjugated

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This gene encodes UDP-galactose-4-epimerase which catalyzes two distinct but analogous reactions: the epimerization of UDP-glucose to UDP-galactose, and the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The bifunctional nature of the enzyme has the important metabolic consequence that mutant cells (or individuals) are dependent not only on exogenous galactose, but also on exogenous N-acetylgalactosamine as a necessary precursor for the synthesis of glycoproteins and glycolipids. Mutations in this gene result in epimerase-deficiency galactosemia, also referred to as galactosemia type 3, a disease characterized by liver damage, early-onset cataracts, deafness and mental retardation, with symptoms ranging from mild ('peripheral' form) to severe ('generalized' form) . Multiple alternatively spliced transcripts encoding the same protein have been identified.

Colocalizes with SMARCA4/BRG1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level) . Expressed in heart and skeletal muscle, but not in liver, spleen, or pancreas.

Cancer, Cancer Metabolism, Carbohydrate Metabolism, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Pathways and Processes, Signal Transduction

Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6- phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP- GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.

1. Maceratesi, P., Daude, N., Dallapiccola, B., Novelli, G., Allen, R., Okano, Y., Reichardt, J.Human UDP-galactose 4-prime epimerase (GALE) gene and identification of five missense mutations in patients with epimerase-deficiency galactosemia. Molec. Genet. Metab. 63: 26-30, 1998. 2. Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM (May 2001) . Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site. J. Biol. Chem. 276 (18) : 15131–6.