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. DUSP7 belongs to a class of DUSPs| designated MKPs| that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795)| JNK (see MIM 601158)| and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes| including cellular proliferation| apoptosis| differentiation| and stress responses (summary by Patterson et al.| 2009
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Număr Catalog 772-BT-AP09372-20ulCategorieAfaceri și industrie > Știință și laboratorFurnizorJiaxing Korain Biotech Ltd (BT Labs)GentaurDimensiune20ulTipsingle