PP185 is a insulin receptor kinase substrate. PP185 undergoes rapid tyrosine phosphorylation, with activity dependent on divalent cations and inhibited by insulin receptor kinase domain antibodies. PP185 can be used for the research of neuroblastoma [1] [2] [3].
In Vitro, PP185 (0.4-200 μM; 1 h) engages an increasing number of cysteine sites in HEK293T cell lysates as its concentration increases, with detectable liganding events observed at higher concentrations[1]. PP185 is phosphorylated in a rapid and dose-dependent manner induced by both Insulin and IGF-I in mouse neuroblastoma N18 cells, with maximal phosphorylation at 1 min and rapid dephosphorylation thereafter[2]. PP185 from rat H-35 hepatoma cells has tyrosine phosphorylation in a cell-free system inhibited by anti-IRK (a site-specific antibody targeting insulin receptor kinase)[3]. PP185 in rat H-35 hepatoma cells undergoes rapid tyrosine phosphorylation induced by insulin treatment[3].
References:
[1]. Biggs GS,et al. Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics. Nat Commun. 2025 Jan 2;16(1):73.
[2]. Shemer J, et al. Insulin and insulin-like growth factor-I stimulate a common endogenous phosphoprotein substrate (pp185) in intact neuroblastoma cells. J Biol Chem. 1987;262(32):15476-15482.
[3]. Tashiro-Hashimoto Y, et al. Tyrosine phosphorylation of pp185 by insulin receptor kinase in a cell-free system. J Biol Chem. 1989;264(12):6879-6885.
In Vitro, PP185 (0.4-200 μM; 1 h) engages an increasing number of cysteine sites in HEK293T cell lysates as its concentration increases, with detectable liganding events observed at higher concentrations[1]. PP185 is phosphorylated in a rapid and dose-dependent manner induced by both Insulin and IGF-I in mouse neuroblastoma N18 cells, with maximal phosphorylation at 1 min and rapid dephosphorylation thereafter[2]. PP185 from rat H-35 hepatoma cells has tyrosine phosphorylation in a cell-free system inhibited by anti-IRK (a site-specific antibody targeting insulin receptor kinase)[3]. PP185 in rat H-35 hepatoma cells undergoes rapid tyrosine phosphorylation induced by insulin treatment[3].
References:
[1]. Biggs GS,et al. Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics. Nat Commun. 2025 Jan 2;16(1):73.
[2]. Shemer J, et al. Insulin and insulin-like growth factor-I stimulate a common endogenous phosphoprotein substrate (pp185) in intact neuroblastoma cells. J Biol Chem. 1987;262(32):15476-15482.
[3]. Tashiro-Hashimoto Y, et al. Tyrosine phosphorylation of pp185 by insulin receptor kinase in a cell-free system. J Biol Chem. 1989;264(12):6879-6885.