Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. Protein phosphatases 2C (PP2Cs) are serine/threonine protein phosphatases primarily involved in stress responses. Two isoforms PP2C α and PP2Cβ are reported. Functionally, PP2C isoforms suppress TGF-β-activated kinase (TAK1), STAT3 and the nuclear factor κB pathway. Anti-Serine/Threonine Protein Phosphatase 2C α/β specifically recognizes 44-46 kDa protein phosphatase 2C α?and β?isoforms.
Immunogen
synthetic peptide corresponding to amino acids 23-37 of the protein phosphatase 2C α/β structural subunit.
Application
The recommended working dilution is 1:1000 to 1:5000 for immunoblotting using peroxidase conjugated goat anti-rabbit IgG and chemiluminescent detection. The recommended working dilution for immunoprecipitation is 1:1000 to 1:5000. The antibody is suitable for protein microarray.
Physical form
Solution in phosphate buffered saline containing 0.08% sodium azide
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Journal of experimental botany, 51(351), 1763-1764 (2000-10-29)
A protein phosphatase 2C (PP2C)-homologous cDNA was isolated from Nicotiana tabacum (NtPP2C1). The deduced protein sequence of 416 amino acids showed the highest degree of similarity to the PP2C of Arabidopsis thaliana (AtPP2CA) implicated in abscisic acid signalling. The expression
ISG15, an interferon-upregulated ubiquitin-like protein, is covalently conjugated to various cellular proteins (ISGylation). In this study, we found that protein phosphatase 2Cbeta (PP2Cbeta), which functions in the nuclear factor kappaB (NF-kappaB) pathway via dephosphorylation of TGF-beta-activated kinase, was ISGylated, and
The Journal of biological chemistry, 279(3), 1739-1746 (2003-10-31)
The NF-kappaB pathway is important in the control of the immune and inflammatory response. One of the critical events in the activation of this pathway is the stimulation of the IkappaB kinases (IKKs) by cytokines such as tumor necrosis factor-alpha
The Journal of biological chemistry, 276(8), 5753-5759 (2000-12-06)
Protein phosphatase 2C (PP2C) is implicated in the negative regulation of stress-activated protein kinase cascades in yeast and mammalian cells. In this study, we determined the role of PP2Cbeta-1, a major isoform of mammalian PP2C, in the TAK1 signaling pathway
The Biochemical journal, 353(Pt 3), 417-439 (2001-02-15)
Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.