Anti-Serine/Threonine Protein Phosphatase 2C α/β antibody produced in rabbit

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.

synthetic peptide corresponding to amino acids 23-37 of the protein phosphatase 2C α/β structural subunit.

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.

Solution in phosphate buffered saline containing 0.08% sodium azide

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