p-Akt1/2/3 Antibody (C-11) is an IgG2b κ mouse monoclonal p-Akt1/2/3 antibody that detects Ser 473 phosphorylated Akt1 and correspondingly Ser 474 phosphorylated Akt2 and correspondingly Ser 472 phosporylated Akt3 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA. p-Akt1/2/3 Antibody (C-11) is available as the non-conjugated anti-p-Akt1/2/3 antibody form, as well as multiple conjugated forms of anti-p-Akt1/2/3 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The serine/threonine kinase Akt family contains several members, including Akt1 (also designated PKB or RacPK), Akt2 (also designated PKBβ or RacPK-β) and Akt 3 (also designated PKBγ or thyoma viral proto-oncogene 3), which exhibit sequence homology with the protein kinase A and C families and are encoded by the c-Akt proto-oncogene. All members of the Akt family have a pleckstrin homology domain. Akt1 and Akt2 are activated by PDGF stimulation. This activation is dependent on PDGFR-β tyrosine residues 740 and 751, which bind the subunit of the phosphatidylinositol 3-kinase (PI 3-kinase) complex. Activation of Akt1 by insulin or insulin-growth factor-1(IGF-1) results in phosphorylation of both Thr 308 and Ser 473. Akt proteins become phosphorylated and activated in insulin/IGF-1-stimulated cells by an upstream kinase(s), and the activation of Akt1 and Akt2 is inhibited by the PI kinase inhibitor wortmannin. Taken together, this data strongly suggests that the protein signals downstream of the PI kinases. Akt3 is phosphorylated on a serine residue in response to insulin. However, the activation of Akt3 by insulin is inhibited by prior activation of protein kinase C via a mechanism that does not require the presence of the PH domain. Akt3 is expressed in 3T3-L1 fibroblasts, adipocytes and skeletal muscle and may be involved in various biological processes, including adipocyte and muscle differentiation, glycogen synthesis, glucose uptake, apoptosis and cellular proliferation.

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