Dual Specificity Phosphatase 19 (DUSP19) is a member of the dual specificity protein phosphatase subfamily. These phosphatases are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP19 is also known by several other names, including TS-DSP1, LMW-DSP3, and SKRP1. This enzyme plays a crucial role in regulating various cellular processes by modulating critical signaling pathways .
DUSP19 is a protein phosphatase that functions as a stress-activated protein kinase pathway-regulating phosphatase. It is involved in the dephosphorylation of specific substrates, thereby modulating their activity and function. The recombinant form of DUSP19 is typically produced in E. coli and includes an N-terminal His-tag for purification purposes .
DUSP19 has been implicated in various cellular processes, including cell growth, differentiation, and apoptosis. It is particularly important in the regulation of the stress-activated protein kinase (SAPK) pathway, which is involved in the cellular response to stress and inflammation . Additionally, DUSP19 has been shown to interact with vascular endothelial growth factor receptor 3 (VEGFR3), playing a role in the regulation of cancer cell invasiveness .