The DUSP13 gene is located on chromosome 10q22.2 and encodes two distinct isoforms through the use of alternative, nonoverlapping open reading frames (ORFs): Testis- and Skeletal Muscle-Specific DSP (TMDP) and Muscle-Restricted DSP (MDSP) . These isoforms share 42% amino acid identity with each other and exhibit high similarity to their mouse counterparts .
DUSP13 is predominantly expressed in skeletal muscle and testis . The TMDP isoform is specifically expressed in testicular germ cells, particularly in spermatocytes and round spermatids, indicating its role in meiosis and differentiation during spermatogenesis . On the other hand, the MDSP isoform is expressed exclusively in skeletal muscle .
Recombinant human DUSP13 has been shown to possess intrinsic phosphatase activity, effectively dephosphorylating synthetic and protein substrates containing either phosphotyrosine or phosphothreonine residues . This activity underscores its importance in cellular signaling and regulation.
Recombinant human DUSP13 is typically produced in Escherichia coli as a single polypeptide chain containing 222 amino acids, with a molecular mass of approximately 24.7 kDa . The recombinant protein is often fused to a His-tag at the N-terminus to facilitate purification using chromatographic techniques .
Recombinant DUSP13 is utilized in various research applications, including studies on signal transduction pathways, cell cycle regulation, and apoptosis. Its ability to dephosphorylate both tyrosine and serine/threonine residues makes it a valuable tool for investigating the intricate mechanisms of cellular regulation.