Anti-GALE monoclonal antibody (DCABH-11662) Made to order

Rabbit anti-Human GALE monoclonal antibody for FC, IP, WB

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Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
Mouse, Rat, Human
Immunogen
A synthetic peptide of human GALE is used for rabbit immunization.
Conjugate
Unconjugated

Target


Alternative Names
GALE; UDP-galactose-4-epimerase; galactose 4 epimerase, UDP; UDP-glucose 4-epimerase; SDR1E1; short chain dehydrogenase/reductase family 1E
Entrez Gene ID
UniProt ID

Product Background


Gene summary
GALE (UDP-Galactose-4-Epimerase) is a Protein Coding gene. Diseases associated with GALE include galactose epimerase deficiency and generalized galactose epimerase deficiency. Among its related pathways are Metabolism and Glycosaminoglycan metabolism. GO annotations related to this gene include protein homodimerization activity and oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor. An important paralog of this gene is UXS1. 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.
Antigen Description
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. Epimerase-deficiency galactosemia (EDG) [MIM:230350]: Clinical features include early-onset cataracts, liver damage, deafness and mental retardation. There are two clinically distinct forms of EDG. (1) A benign, or peripheral form with no detectable GALE activity in red blood cells and characterized by mild symptoms. Some patients may suffer no symptoms beyond raised levels of galactose-1-phosphate in the blood. (2) A much rarer generalized form with undetectable levels of GALE activity in all tissues and resulting in severe features such as restricted growth and mental development. Note=The disease is caused by mutations affecting the gene represented in this entry. The function about GALE antigen include UDP-glucose 4-epimerase activity; UDP-glucose 4-epimerase activity; UDP-glucose 4-epimerase activity; catalytic activity; coenzyme binding; isomerase activity; nucleotide binding; protein homodimerization activity.
Pathway
Amino sugar and nucleotide sugar metabolism, organism-specific biosystem; Amino sugar and nucleotide sugar metabolism, conserved biosystem; Galactose catabolism, organism-specific biosystem; Galactose metabolism, organism-specific biosystem; Galactose metabolism, conserved biosystem; Metabolic pathways, organism-specific biosystem; Metabolism, organism-specific biosystem.

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References


Drgas-Burchardt, E; Switalski, Z; et al. A number of stable matchings in models of the Gale-Shapley type. DISCRETE APPLIED MATHEMATICS 161:2932-2936(2013).
Inall, M; Boyd, T; et al. AUV observations of surface mixing and bubble entrainment in the Clyde estuary, Scotland. 2012 IEEE/OES AUTONOMOUS UNDERWATER VEHICLES (AUV) :-(2012).

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