TCPTP Protein, Human (sf9, His-GST)

TCPTP, a non-receptor type tyrosine-specific phosphatase, acts as a crucial regulator by dephosphorylating various receptor and non-receptor protein tyrosine kinases, including INSR, EGFR, CSF1R, PDGFR, JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3, and STAT6, either in the nucleus or the cytoplasm. This phosphatase exerts negative control over diverse signaling pathways and biological processes such as hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. In the immune system, TCPTP plays a multifaceted role, influencing T-cell receptor signaling by dephosphorylating FYN and LCK to regulate T-cell differentiation and activation. Additionally, it negatively modulates cytokine-mediated signaling, including IL2, interferon, IL6, and IL4 pathways. Beyond immune regulation, TCPTP participates in anchorage-dependent, negative regulation of EGF-stimulated cell growth and PDGF receptor-beta signaling, thus influencing cell proliferation. Moreover, it plays a vital role in glucose homeostasis, negatively regulating the insulin receptor signaling pathway and controlling gluconeogenesis and liver glucose production through the IL6 signaling pathway. TCPTP's broad impact underscores its significance in diverse cellular processes, and it may also have DNA binding capabilities.