Dual specificity protein phosphatase 9, Mitogen-activated protein kinase phosphatase 4, MAP kinase phosphatase 4, MKP-4, DUSP9, MKP4
DUSP9 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. DUSP9 shows selectivity for members of the ERK family of MAP kinases, is expressed only in placenta, kidney, and fetal liver, and is localized to the cytoplasm and nucleus.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP8452a was selected from the N-term region of human DUSP9. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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