PTP4A2 Human

PTP4A2 contains a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif . The prenylation motif allows the enzyme to associate primarily with the plasma and endosomal membranes . This association is crucial for its function in cellular signaling pathways.

The enzyme has been shown to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), suggesting that it may regulate GGT II activity . Overexpression of PTP4A2 in mammalian cells has been associated with a transformed phenotype, indicating its potential role in tumorigenesis .

PTP4A2 plays a significant role in protein dephosphorylation, a process essential for regulating cell growth, development, differentiation, survival, and migration . The enzyme’s activity is involved in various biological processes, including post-translational protein modification and peptidyl-tyrosine dephosphorylation .

The human recombinant form of PTP4A2 is often expressed in E. coli systems for research purposes . This recombinant protein is useful for studying enzyme kinetics, screening inhibitors, and selectivity profiling . It is typically formulated in a buffer containing Tris-HCl, NaCl, Tween-20, glycerol, and DTT to maintain its stability and activity .

Due to its regulatory roles in cellular processes, PTP4A2 is a valuable target for research in cancer biology and cell signaling. Researchers utilize the recombinant form to investigate its function, interactions, and potential as a therapeutic target .