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 [PubMed 19228121]).[supplied by OMIM, Dec 2009].
custom-made
DUSP18
宿主: 人
宿主: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
ELISA, SDS, WB
custom-made
DUSP18
宿主: 小鼠
宿主: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
ELISA, SDS, WB