Anti-Serine/Threonine Protein Phosphatase 2 A/B′ pan2 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 – B, B′ and B”. Members of the B′/B56/PR61 family regulatory subunits of PP2A determine the subcellular localization, substrate specificity, and catalytic activity of PP2A in a wide range of biological processes. B′/B56/PR61 are reportedly involved in major signaling pathways such as Wnt, Hedgehog and planar cell polarity pathway
Anti-serine/threonine protein phosphatase 2A/B′ pan 2 recognizes an epitope common to the ~56 kDa protein phosphatase 2A B′ subunits from rat brain.

synthetic peptide (VSSPHFQVAERALY) corresponding to the N-terminus of the protein phosphatase 2A/B′ pan2 subunit.

Anti-protein phosphatase 2A/B′ Pan 2 antibody may be used for immunoblotting at a working dilution of 1:500-1:1000 in total rat brain homogenate. The antibody is suitable for protein microarray.

Solution in phosphate buffered saline containing 0.08% sodium azide.

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