Recombinant Human PRL-1 protein

Supplementary information

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

PRL-1 also known as phosphatase of regenerating liver-1 or DIFMU-P is an enzyme that functions as a phosphatase. It has a molecular mass of approximately 20 kDa. PRL-1 is actively expressed in various tissues including the liver and skeletal muscle where it plays significant roles in cellular processes. Mechanically it exhibits a dual specificity for both tyrosine and serine/threonine residues enabling it to dephosphorylate target proteins which can regulate diverse signaling pathways.

Biological function summary

PRL-1 plays an important role in cell proliferation differentiation and migration. Its activity impacts cellular motility making it important for physiological and pathological processes. While PRL-1 primarily acts as a monomer it can also form complexes with other proteins amplifying its biological effects. Elevation in PRL-1 expression levels correlates with enhanced migratory capacity of tumor cells suggesting a role in cancer progression.

Pathways

Various cellular functions involve PRL-1 which participates in the MAPK and PI3K/Akt pathways. These pathways are critical in regulating cell cycle and survival. PRL-1's relation to proteins like AKT1 and ERK1/2 highlights its contribution to intracellular signaling cascades that drive growth and survival responses in cells. PRL-1's phosphatase activity influences these pathways by modulating the phosphorylation status of various substrate proteins impacting downstream signaling.

Increased expression of PRL-1 relates to cancer particularly colorectal and breast cancers. Its role in promoting cell proliferation and migration makes it a target of interest for cancer research. PRL-1 is connected with proteins such as p53 and E-cadherin within these contexts correlating with the loss of cell-cell adhesion and increased invasive characteristics in tumor cells. Targeting PRL-1 could provide therapeutic benefits in managing cancer-associated pathologies.