Description
GALE Antibody | 62-529 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: Predicted species reactivity based on immunogen sequence: Bovine, Mouse
Immunogen: 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.
Research Area: Cancer, Obesity, Signal Transduction
Tested Application: WB, IHC-P, IF, Flow
Application: For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:50~100
For FACS starting dilution is: 1:10~50
For IF starting dilution is: 1:10~50
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 38 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: 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)
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: 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.