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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 (11) and many more products for this protein.
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JNK (show MAPK8 Antibodies) and DUSP18 reciprocally modulate the SUMOylation, which plays a regulatory role in the aggregation of ataxin-1 (show ATXN1 Antibodies).
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 Antibodies)/JNK (show MAPK8 Antibodies) 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