DUSP3 Antibody

Dual-specificity phosphatase 3, also called VHR, is a member of the dual specificity protein phosphatase subfamily. DUSPs constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP3 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs. The DUSP3 gene is mapped on 17q21.31. Confocal microscopy demonstrated that phosphorylated VHR accumulated at the immune synapse between the T cell and the antigen-presenting cell in the presence of antigen. Tyrosine phosphorylation of VHR affects protein-protein interaction, subcellular location, or substrate targeting, given that tyr138 is located on the opposite side of the VHR catalytic center.