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Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. Additionally we are shipping DUSP18 Proteins (9) and DUSP18 Antibodies (4) and many more products for this protein.
The crystal structure of human DSP18 (official symbol DUSP18) has been determined at 2.0 A resolution.
DUSP18 appears to serve an important role by regulation of SAPK (show MAPK9 ELISA Kits)/JNK (show MAPK8 ELISA Kits) pathway
Dual-specificity phosphatases (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. They have been implicated as major modulators of critical signaling pathways. DUSP18 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 (see MIM 600714) (summary by Patterson et al., 2009
dual specificity phosphatase 18
, dual specificity protein phosphatase 18
, low molecular weight dual specificity phosphatase 20