Anti-Serine/Threonine Protein Phosphatase 2 A/Bγ 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 phosphatase 2A (PP2A) holozyme consists of a catalytic subunit (C), a structural subunit (A) and a regulatory subunit (B). The subunit B dictates the substrate specificity and is coded by at least 13 genes resulting in 3 distinct classes of subunits - α, β and γ. The B γ subunit is targeted to the nucleus. The PP2A holoenzyme has been implicated in various functions such as cell cycle progression, oncogenic transformation and is subjected to tight regulation at the translational level, by post translational modifications and by protein-protein interations.
Anti-Serine/Threonine Protein Phosphatase 2A/B γ specifically recognizes 56 kDa protein phosphatase 2A/B γ isoforms.

synthetic peptide (REPSKNAPHSQGE) corresponding to the internal conserved sequence (amino acids 53-66) of mammalian protein phosphatase 2 A/B γ.

The recommended concentration for detection by immunoblotting is 1-10 μg/mL using peroxidase conjugated goat anti-rabbit IgG and chemiluminescent detection.

Solution in phosphate buffered saline, pH 7.2-7.4, containing 0.08% sodium azide.