Protein kinase B or Akt (PKB/Akt) is a serine/threonine kinase, which in mammals comprises three highly homologous members known as PKB alpha (Akt1), PKB beta (Akt2) and PKB gamma (Akt3). PKB/Akt is a growth-factor-regulated protein kinase which contains a pleckstrin homology (PH) domain. Binding of phosphoinositide 3-OH kinase products to the pleckstrin homology domain results in translocation of PKB/Akt to the plasma membrane where it is activated by phosphorylation by upstream kinases including the phosphoinoside-dependent kinase 1 (PDK1). Key roles for this enzyme can be found in cellular processes such as glucose metabolism, cell proliferation, apoptosis, transcription and cell migration.
Human protein kinase Akt3/PKBgamma, recombinantly expressed. Mw 58.7 kDa. Purity >95% by SDS-PAGE. Specific activity > 50.000 Units/mg (1 Unit = 1 pmol/min transferred to synthetic peptide RPRAATF at 30 degree Celsius). No protease activity detectable.
Size: 20 µg
Ordering information: shipped on dry ice
Product specific literature references:
Barthel A, Nakatani K, Dandekar AA, Roth RA (1998) "Protein kinase C modulates the insulin-stimulated increase in Akt1 and Akt3 activity in 3T3-L1 adipocytes" Biochem. Biophys. Res. Commun. 243(2):509-13
Masure S, Haefner B, Wesselink JJ, Hoefnagel E, Mortier E, Verhasselt P, Tuytelaars A, Gordon R, Richardson A (1999) "Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3" Eur. J. Biochem. 265(1):353-60
Brodbeck D, Cron P, Hemmings BA (1999) "A human protein kinase Bgamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain" J. Biol. Chem. 274(14):9133-6
Nakatani K, Sakaue H, Thompson DA, Weigel RJ, Roth RA (1999) "Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site" Biochem. Biophys. Res. Commun. 257(3):906-10
Okano J, Gaslightwala I, Birnbaum MJ, Rustgi AK, Nakagawa H (2000) "Akt/protein kinase B isoforms are differentially regulated by epidermal growth factor stimulation" J. Biol. Chem. 275(40):30934-42
Brodbeck D, Hill MM, Hemmings BA (2001) "Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain" J. Biol. Chem. 276(31):29550-8
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