Activation of cell growth leads to the multiple phosphorylation of 40S ribosomal protein S6. The kinase responsible for controlling this event is termed p70S6K (1). Northern blot analysis shows p70S6K to be ubiquitously expressed in human adult tissues. p70S6K is activated by serum stimulation, and the serum-induced activation is inhibited by wortmannin and rapamycin. p70S6k activity undergoes changes in the cell cycle and increases 20-fold in G1 cells released from G0 (2). The kinase is reactivated 10-fold when cells released from a nocodazole-induced metaphase block enter G1 of the next cell cycle. The immunosuppressive agent rapamycin induces inactivation of p70s6k with no effect on other mitogen-activated kinases (3). The principal targ
Size
100 μg
Concentration
5μg/50 μl
Applications
RUO
Other Names
p70, Ribosomal protein S6 kinase beta-1, Serine/threonine-protein kinase 14A