Recombinant Human DUSP13 protein

DUSP13 (Dual Specificity Phosphatase 13), also known as MDSP or TMDP, is a member of the dual-specificity phosphatase family, which regulates mitogen-activated protein kinase (MAPK) signaling pathways by dephosphorylating both phosphotyrosine and phosphoserine/phosphothreonine residues. It belongs to the atypical DUSP subfamily due to its unique structural features, including a conserved C-terminal catalytic phosphatase domain and a divergent N-terminal region lacking MAPK-binding motifs found in typical MAPK phosphatases (MKPs).

DUSP13 exists in two splice variants: DUSP13A (expressed predominantly in skeletal muscle and heart) and DUSP13B (testis-specific). Its recombinant form is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems to study its enzymatic activity, substrate specificity, and interactions. Recombinant DUSP13 exhibits selectivity toward stress-activated MAPKs, particularly p38 and JNK, implicating its role in cellular stress responses, apoptosis, and muscle differentiation.

Research highlights its involvement in pathophysiological contexts, such as cancer, metabolic disorders, and inflammation. For instance, DUSP13 overexpression in certain cancers modulates chemoresistance by altering MAPK-driven survival pathways. Structural studies using recombinant DUSP13 have revealed insights into its catalytic mechanism and regulatory regions, enabling the design of mutants (e.g., catalytically inactive Cys-to-Ser variants) for functional assays.

Recombinant DUSP13 is also explored for therapeutic targeting, as small-molecule inhibitors or activators could fine-tune MAPK signaling in diseases with dysregulated stress responses. Further studies aim to clarify its tissue-specific roles and post-translational modifications, leveraging recombinant protein tools to advance mechanistic and translational discoveries.