Recombinant Staphylococcus aureus 30 kDa neutral phosphatase protein (His tag)

Supplementary information

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

The 30 kDa neutral phosphatase also known as 30 kDa protein is an enzyme that plays a mechanical role in dephosphorylation facilitating the removal of phosphate groups from proteins. With a molecular mass of approximately 30 kilodaltons (kDa) this phosphatase is expressed in a variety of tissues with significant activity observed in liver and muscle cells. It functions by modulating the phosphorylation status of its target proteins affecting the activity and function of these proteins within cellular processes.

Biological function summary

The 30 kDa neutral phosphatase regulates several cellular processes through its enzymatic activity. It is not defined as a part of a larger protein complex but operates independently to influence signal transduction pathways. This phosphatase modulates enzyme activity impacting cell cycle progression DNA repair and cell growth responses. Its function is vital to maintaining homeostasis within the cellular environment balancing the phosphorylation state of numerous intracellular proteins.

Pathways

The 30 kDa neutral phosphatase integrates into various signal transduction and metabolic pathways. It participates in the MAPK/ERK pathway which affects cellular response to growth signals and stress stimuli. Additionally it interacts with proteins in the insulin signaling pathway which is essential for glucose uptake and metabolism. The phosphatase exerts its influence by modifying key signaling molecules like kinases within these pathways influencing downstream biological effects.

Disruptions in the function of the 30 kDa neutral phosphatase are linked to metabolic disorders and cancer. Aberrant activity can contribute to the development of type 2 diabetes due to its role in insulin signaling affecting glucose metabolism and homeostasis. Additionally dysregulation of its enzymatic activity associates with proliferative disorders such as cancer where it interacts with proteins that regulate cell division and growth like cyclins. Such links make this phosphatase a potential target for therapeutic interventions in these disease contexts.