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Phospho-DUSP16 (Ser446) Polyclonal Antibody detects endogenous levels of DUSP16 only when phosphorylated at Ser446.
Dual-specificity phosphatases 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. DUSP16 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK proteins ERK, JNK, and p38 with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25-like domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Dual specificity protein phosphatase 16; MAP kinase phosphatase 7; MAP kinase phosphatase-7; map kinase phosphatase-M; MAPK phosphatase-7; MGC129701; MGC129702; Mitogen-activated protein kinase phosphatase 7
Gene Aliases: 3830417M17Rik; AW558566; D6Ertd213e; DUSP16; KIAA1700; MKP-7; MKP7; Mkpm
UniProt ID: (Human) Q9BY84
Entrez Gene ID: (Human) 80824, (Mouse) 70686
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