Human PTPN12 ELISA Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The Protein Tyrosine Phosphatase Non-Receptor Type 12 (PTPN12) often referred to as PTP-PeST is an enzyme that plays a significant mechanical role within cells. PTPN12 is part of the protein tyrosine phosphatase (PTP) family which is responsible for removing phosphate groups from phosphotyrosine residues on proteins. This activity regulates many cellular processes including growth and differentiation. PTPN12 has a molecular mass of approximately 86 kDa. It is ubiquitously expressed in various tissues but shows higher expression in hematopoietic cells.

Biological function summary

As a non-receptor type phosphatase PTPN12 partners with several proteins to perform essential cellular functions. It interacts with multiple components in the cell participating in the assembly of protein complexes that manage cytoskeletal dynamics and cell movement. PTPN12 influences signal transduction pathways by interacting with adapter proteins such as p130Cas and Paxillin which are vital for cell adhesion and migration. It also plays a role in maintaining cellular homeostasis by controlling signaling cascades that prevent excessive cell proliferation.

Pathways

PTPN12 takes part in critical signal transduction networks most notably the Integrin signaling and RhoA pathways. In the Integrin pathway PTPN12 negatively regulates signaling by dephosphorylating focal adhesion-associated proteins. This regulation affects cell attachment to the extracellular matrix and cell motility. The interaction of PTPN12 with proteins such as Src and FAK (Focal Adhesion Kinase) illustrates its involvement in these processes. In the RhoA pathway PTPN12 influences cytoskeletal rearrangement and cell shape regulation linking to its role in cell migration.

Associated diseases and disorders

Disruptions in PTPN12 function associate with cancer progression such as breast cancer and inflammatory disorders. In breast cancer physiological studies indicate that PTPN12 acts as a tumor suppressor. Its loss or reduced activity may lead to unregulated cell proliferation and metastasis by failing to restrain pathways involving Src and FAK. In inflammatory disorders altered activities of PTPN12 can affect immune cell function contributing to conditions like rheumatoid arthritis. The enzyme's dysfunction can amplify inflammatory signals through faults in the regulation of immune cells linking PTPN12 to increased disease susceptibility.