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Anti-phospho-Akt (Ser473) Antibody, clone 6F5
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REFERENCES
PDK1, one of the missing links in insulin signal transduction?
Cohen, P, et al. (1997) FEBS Lett., 410: 3-10 (1997)
Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation.
James, S R, et al. (1996) Biochem. J., 315 ( Pt 3): 709-13 (1996)
3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase.
Alessi, D R, et al. (1997) Curr. Biol., 7: 776-89 (1997)
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B.
Cross, D A, et al. (1995) Nature, 378: 785-9 (1995)
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Species Reactivity Key Applications Host Format Antibody Type
H, M, R, Vrt ELISA, WB, FC, IF, IHC Mouse Purified Monoclonal Antibody
Description:
Anti-phospho-Akt (Ser473) Antibody, clone 6F5
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Specificity:
Recognizes Akt only when phosphorylated on Ser473. This antibody does not cross-react with Akt1/PKBα when it is not phosphorylated on Ser473.
Molecular Weight:
60 kDa
Epitope:
Phosphorylated Ser473
Immunogen:
Peptide encompassing and including phosphorylated Ser473 of human Akt1.
Modifications:
Phosphorylation
Clone:
6F5
Isotype:
IgG1κ
Background Information:
Akt/PKB is a Ser/Thr kinase and a major known effecter of the PI3 Kinase pathway. It is involved in multiple signaling pathways that relate to many biological processes including glucose metabolism, cell survival/apoptosis, cell cycle control, angiogenesis, differentiation, and cell growth and proliferation. In mammals three isoforms of Akt (Akt1/PKB, Akt2/PKB, and Akt3/PKB)exists. They exhibit a high degree of homology, but differ slightly in the localization of their regulatory phosphorylation sites. Akt is the predominant isoform that is in most tissues and is thought to have a dominant role in growth, survival, embryonic development, and adipocyte differentiation. Akt2 is correlated with the regulation of glucose homeostasis and is the predominant isoform expressed in insulin-responsive tissues. Akt3 is abundant in brain tissue. Each Akt isoform is composed of three functionally distinct regions: an N-terminal Pleckstrin Homology (PH) domain that provides a lipid-binding module to direct Akt to PIP3 at the cell membrane that is necessary for its activation, a central catalytic domain containing Thr308, and a C-terminal hydrophobic motif containing Ser473. The activation of Akt is dependent on a dual regulatory mechanism that requires both its translocation to the plasma membrane and dual phosphorylation on Thr308 and Ser473 by PDK1 and the TORC2 complex, respectively.
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Species Reactivity:
Human
Mouse
Rat
Vertebrates
Species Reactivity Note:
Human, mouse, and rat tested. Expected to react with most species as sequence is 100% homologous with most common vertebrate.
Application Notes:
Immunofluroescence Analysis:
EGF-treated A431 cells were fixed, permeabilized, and stained with Anti-phospho-Akt (Ser473), clone 6F5 (2 μg/mL) (red). Cy3-conjugated anti-mouse was used for detection and Phalloidin-AlexaFluor®488 (green) was used to stain actin.
Immunohistochemistry:
Anti-phospho-Akt (Ser473), clone 6F5 was diluted to 1:200, IHC-Select Detection with HRP-DAB.
Flow Cytometry:
Anti-phospho-Akt (Ser473) was used at a 1:800 dilution for this assay.
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Quality Assurance:
Western Blot Analysis:
0.5-1 μg/mL of this lot dete |