DUSP7: Proteins and Enzymes
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-basedprotein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosineand 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) withspecificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domainand an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologicprocesses, including cellular proliferation, apoptosis, differentiation, and stress responses (summary by Patterson etal., 2009 (PubMed 19228121)).(supplied by OMIM)
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2 results for "DUSP7 Proteins and Enzymes" in Products
2 results for "DUSP7 Proteins and Enzymes" in Products
DUSP7: Proteins and Enzymes
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-basedprotein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosineand 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) withspecificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domainand an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologicprocesses, including cellular proliferation, apoptosis, differentiation, and stress responses (summary by Patterson etal., 2009 (PubMed 19228121)).(supplied by OMIM)
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| Applications: | WB, ELISA, MA, AP |
| Applications: | AC |