Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate. Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells, which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers. Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo. Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells.
The antibody was affinity-purified from mouse ascites fluids or tissue culture supernatant by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB 1:2000, IHC 1:150
Application Notes:
IgG2a
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