Anti-DUSP3 Antibody Picoband® Fluoro488 Conjugated

DUSP3 (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.

Amino Acid Metabolism, Amino Acids, Cancer, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Protein Phosphorylation, Ser/Thr Phosphatases, Signal Transduction, Tyrosine Phosphatases

Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2. .

1. Alonso, A., Rahmouni, S., Williams, S., van Stipdonk, M., Jaroszewski, L., Godzik, A., Abraham, R. T., Schoenberger, S. P., Mustelin, T. Tyrosine phosphorylation of VHR phosphatase by ZAP-70. Nature Immun. 4: 44-48, 2003. 2. Ishibashi, T., Bottaro, D. P., Chan, A., Miki, T., Aaronson, S. A. Expression cloning of a human dual-specificity phosphatase. Proc. Nat. Acad. Sci. 89: 12170-12174, 1992. 3. Patterson, K. I., Brummer, T., O'Brien, P. M., Daly, R. J. Dual-specificity phosphatases: critical regulators with diverse cellular targets.Biochem. J. 418: 475-489, 2009.