Phospho-(Ser/Thr) Akt Substrate Antibody preferentially recognizes peptides and proteins containing phospho-Ser/Thr preceded by Lys/Arg at positions -5 and -3, in a manner largely independent of other surrounding amino acids. Some cross-reactivity is observed for peptides that contain phospho-Ser/Thr preceded by Arg/Lys at positions -3 and -2. No cross-reactivity is observed with the corresponding nonphosphorylated sequences or with other phospho-Ser/Thr-containing motifs. By ELISA, the antibody recognizes a wide range of phosphorylated Akt substrate peptides, and, by 2-D gel Western blot analysis, it recognizes a large number of proteins presumed to be Akt substrates. (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)
Source / Purification
Polyclonal antibodies are produced by immunizing animals with phospho-Akt substrate peptides . Antibodies are purified by protein A and peptide affinity chromatography.
Background
An important class of kinases, referred to as Arg-directed kinases or AGC-family kinases, includes cAMP-dependent protein kinase (PKA), cGMP-dependent protein kinase (PKG), protein kinase C, Akt, and RSK. These kinases share a substrate specificity characterized by Arg at position -3 relative to the phosphorylated Ser or Thr (1,2). Akt plays a central role in mediating critical cellular responses including cell growth and survival, angiogenesis, and transcriptional regulation (3-5). While a number of Akt substrates are known (such as GSK-3, Bad, and caspase-9) many important substrates await discovery. Akt phosphorylates substrates only at Ser/Thr in a conserved motif characterized by Arg at positions -5 and -3 (6). Phospho-Akt substrate-specific antibodies from CST are powerful tools for investigating the regulation of phosphorylation by Akt and other Arg-directed kinases, as well as for high throughput kinase drug discovery.
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