GALE antibody

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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.
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Product specifications
Category | Primary Antibodies |
Immunogen Target | UDP-galactose-4-epimerase (GALE) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | WB: 1:500 - 1:2000; IHC: 1:50 - 1:200; IF: 1:10 - 1:100 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 36 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IHC, IF |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months (Avoid repeated freeze / thaw cycles.) |
UniProt ID | Q14376 |
Gene ID | 2582 |
Alias | UDP-glucose 4-epimerase,Galactowaldenase,UDP-N-acetylgalactosamine 4-epimerase (UDP-GalNAc 4-epimerase),UDP-N-acetylglucosamine 4-epimerase (UDP-GlcNAc 4-epimerase),UDP-galactose 4-epimerase,GALE |
Background | Antibody anti-GALE |
Status | RUO |
Note | Mol. Weight 36 kDa |
Descripción
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GALE antibody
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.
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