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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 DUSP19 Antibodies (35) and many more products for this protein.
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the activity of JNK (show MAPK8 Proteins) stimulated by leptin (show LEP Proteins) was suppressed by DUSP19 overexpression.
crystal structure of SKRP1 (C150S) has been determined and refined at 1.26 A resolution (Table I). The structure reveals 142 residues (residues 65-206) of SKRP1 and three ions (two sulfates and one phosphate) at the catalytic site
LMW-DSP3 was expressed in the heart, lung, liver, and pancreas, and the expression level in the pancreas was highest. The LMW-DSP3 gene was located in human chromosome 2q32, and consisted of five exons spanning 21kb of human genomic DNA[LMW-DSP3]
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. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and 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 19
, dual specificity protein phosphatase 19
, dual specificity protein phosphatase 19-like
, SAPK pathway-regulating phosphatase 1
, dual specificity phosphatase TS-DSP1
, low molecular weight dual specificity phosphatase 3
, protein phosphatase SKRP1
, stress-activated protein kinase pathway-regulating phosphatase 1