mouse monoclonal IgG1; methyl-PP2A-Cα/β Antibody (2A10) is an IgG1 κ mouse monoclonal methyl-PP2A-C alpha / beta antibody (also designated protein phosphatase 2 catalytic subunit alpha antibody) that detects the methyl-PP2A-C alpha / beta protein of mouse, rat, human and chicken, d, S. cerevisiae origin by WB and IP. methyl-PP2A-Cα/β Antibody (2A10) is available as both the non-conjugated anti-methyl-PP2A-C alpha / beta antibody form, as well as multiple conjugated forms of anti-methyl-PP2A-C alpha / beta antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aα and PP2Aβ. The PP2A catalytic subunit associates with a variety of regulatory subunits. Regulatory subunits include PP2A-Aα and -Aβ, PP2A-Bα and -Bβ, PP2A-Cα and -Cβ, PP2A-B56α and -B56β. Reversible carboxymethylation of the C-terminal leucine residue (Leu309) of the PP2A catalytic subunit (PP2A-Cα/β) in vitro has been shown to regulate catalytic activity. It has been suggested that this posttranslational modification may play a role in assembly of the holoenzyme.