|Application ||WB, IHC-P, FC, IF, E|
|Other Accession||Q8R059, Q3T105|
|Calculated MW||38282 Da|
|Antigen Region||142-171 aa|
|Other Names||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 (HGNC:4116)|
|Target/Specificity||This GALE antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 142-171 amino acids from the Central region of human GALE.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GALE Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
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Provided below are standard protocols that you may find useful for product applications.
UDP-galactose-4-epimerase 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.
Openo,K.K., et.al., Am. J. Hum. Genet. 78 (1), 89-102 (2006)
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