Description
GSTA3 Antibody | 16-957 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 1-222 of human GSTA3 (NP_000838.3) .
Research Area: Cancer, Cell Cycle, Growth Factors, Signal Transduction
Tested Application: WB, IF
Application: WB: 1:500 - 1:2000
IF: 1:50 - 1:100
Specificiy: N/A
Positive Control 1: PC-3
Positive Control 2: 293T
Positive Control 3: Mouse lung
Positive Control 4: Mouse liver
Positive Control 5: Mouse kidney
Positive Control 6: Rat kidney
Molecular Weight: Observed: 25kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: GSTA3, GST class-alpha member 3, GSTA3-3, Glutathione S-transferase A3, GTA3, Glutathione S-transferase A3-3
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-tranferase belonging to the alpha class genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined. [provided by RefSeq, Jul 2008]