MKP3 Antibody detects endogenous levels of total MKP3 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human MKP3. Antibodies are purified by protein A and peptide affinity chromatography.
Background
MAP kinases are inactivated by dual-specificity protein phosphatases known as MAPK phosphatases (MKP), that differ in their substrate specificity, tissue distribution, inducibility by extracellular stimuli and cellular localization. MKPs specifically dephosphorylate both threonine and tyrosine residues in MAPK P-loops and have been shown to play important roles in regulating the function of the MAPK family (1,2). At least 13 members of the family (MKP-1, PAC-1, VHR, MKP-2, HVH3, MKP-3, PYST2, HVH5, MKP-4, MKP-5, MKP-6, MKP-7, DSP2) display unique substrate specificities for various MAP kinases (3). MAPK phosphatases typically contain an amino-terminal rhodanese-fold responsible for MKP docking to MAPK family members and a carboxy-terminal catalytic domain (4). These phosphatases can play important roles in development, immune system function, stress responses and metabolic homeostasis (5), and also in the development of cancer and the response of cancer cells to chemotherapy (6).