GALE Antibody (Clone AT6G10)

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 enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Additionally, human and some bacterial GALE isoforms reversibly catalyze the formation of UDP-N-acetylgalactosamine (UDP-GalNAc) from UDP-N-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis.
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Properties

Data Sheet Click for Datasheet
Catalog Number MA01265
Size 100 µL
Host Type Mouse
Immunogen Recombinant human GALE (1-348aa) purified from E. coli
Specificity
Isotype Mouse IgG1, k
Reacitivity Human
Clone Anti-human GALE mAb, clone AT6G10, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human GALE protein.
Uniprot
Concentration 1mg/ml
Dilution
Formulation Liquid. In Phosphate-Buffered Saline (pH 7.4) with 0.02% Sodium Azide, 10% Glycerol.
Application ELISA, WB, Flow cytometry, ICC/IF
Other Names uDP-glucose 4-epimeraes, SDR1E1.uDP-glucose 4-epimeraes, uDP-galactose 4-epimerase, Galactowaldenase, FLJ95174, FLJ97302
Storage Lyophilized product: 5 years at 2 - 8°C; Solution: 2 years at -20°C.
Postscript For research use only, not for use in diagnostic procedures.

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