Prostatic acid phosphatase/ACPP Protein, Human (HEK293, His, solution)

PPAP protein (cPAcP), a nonspecific tyrosine phosphatase and prostate epithelial differentiation antigen, is involved in regulating prostate epithelial growth. PPAP dephosphorylates a variety of substrates under acidic conditions (pH 4-6) and leads to the inactivation of lysophosphatidic acid in seminal plasma. It interacts with and dephosphorylates ErbB-2 primarily at Tyr(1221/2), thereby blocking downstream signaling and resulting in reduced cell growth. It also functions as a negative growth regulator of prostate cancer (PCa) cells in part through dephosphorylation of ErbB-2. The PPAP protein is often used as a biomarker for prostate cancer. Inhibition of prostate cancer development through ERBB2 dephosphorylation and inactivation of MAPK-mediated signaling. Therefore, the occurrence of androgen-independent cell proliferation and tumorigenicity is closely related to the reduction of intracellular PPAP protein expression. Intratumoral injection of a PAcP cDNA expression vector inhibits xenograft tumor progression and reduces ErbB-2 tyrosyl phosphate. In prostate cancer and PCa cells with reduced cPAcP, reduced cPAcP leads to activation of ErbB-2 and ERK1/2 signaling.