Phospho-AKT1 (T450) Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of Phospho-AKT1(T450) on MCF-7 cells lysates using anti-Phospho-AKT1(T450) antibody at 1/1,000 dilution.
Fig2: Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using anti-Phospho-AKT1(T450) antibody. Counter stained with hematoxylin.
Host Species; Species ReactivityRabbit; Human, Mouse, Rat
ImmunogenSynthetic phospho-Peptide corresponding to residues surrounding Thr450 of human AKT1.
Application SummaryWB, IHC, IP
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesRAC-alpha serine/threonine-protein kinase, Protein kinase B, Protein kinase B alpha, Proto-oncogene c-Akt, RAC-PK-alpha
BackgroundThe serine/threonine kinase Akt family contains several members, including Akt1 (also designated PKB or RacPK), Akt2 and Akt 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. Phosphorylation of both residues is important to generate a high level of Akt1 activity, and the phosphorylation of Thr 308 is not dependent on phosphorylation of Ser 473 in vivo. Thus, Akt proteins become phosphorylated and activated in insulin/IGF-1-stimulated cells by an upstream kinase(s). The activation of Akt1 and Akt2 is inhibited by the PI kinase inhibitor wortmannin, suggesting that the protein signals downstream of the PI kinases.(ET1612-73)