DUSP10 Human

DUSP10 is a dual specificity phosphatase that inactivates its target kinases by removing phosphate groups from both serine/threonine and tyrosine residues. This action is crucial for the regulation of the Mitogen-Activated Protein Kinase (MAPK) signaling pathways, which are involved in various cellular processes such as proliferation, differentiation, and stress responses .

The recombinant form of DUSP10 is typically produced in Escherichia coli (E. coli) and is often tagged with a His-tag at the N-terminus to facilitate purification. The recombinant protein corresponds to amino acids 149-482 of the human DUSP10 sequence .

DUSP10 specifically targets and dephosphorylates members of the MAPK family, including p38 MAPK and JNK/SAPK, with a higher selectivity for p38 MAPK. This selective dephosphorylation is significant because it helps regulate the cellular responses to stress and inflammatory cytokines .

The specific activity of recombinant DUSP10 is measured by its ability to hydrolyze p-nitrophenyl phosphate (pNPP) at a defined rate. For instance, one unit of enzyme activity is defined as the amount of enzyme that hydrolyzes 1.0 nmole of pNPP per minute at pH 7.5 and 37°C .

Recombinant DUSP10 is used in various research applications, including:

• Studying MAPK signaling pathways: By understanding how DUSP10 regulates these pathways, researchers can gain insights into cellular processes and disease mechanisms.
• Drug discovery: DUSP10 is a potential target for therapeutic interventions in diseases where MAPK signaling is dysregulated, such as cancer and inflammatory diseases.
• Biochemical assays: The enzyme’s activity can be measured in vitro to study its kinetics and interactions with other proteins .

Recombinant DUSP10 is typically stored in a buffer containing Tris-HCl, DTT, glycerol, and NaCl to maintain its stability. It is recommended to store the protein at 4°C for short-term use and at -20°C for long-term storage, avoiding freeze-thaw cycles to preserve its activity .