Render Target: SSR
Render Timestamp: 2025-03-15T21:11:23.276Z
Commit: a619ae74f66dae0f27639e88da12bcf600e46428
XML generation date: 2025-03-07 13:14:15.584
Product last modified at: 2025-02-21T08:00:59.711Z
Cell Signaling Technology Logo
1% for the planet logo
PDP - Template Name: Cell Extracts
PDP - Template ID: *******b5396df

p70 S6 Kinase Control Cell Extracts #9203

We recommend the following alternatives

Inquiry Info. # 9203

Please see our recommended alternatives.

    Product Information

    Storage

    Store at -20°C. Supplied in SDS Sample Buffer: 62.5 mM Tris- HCl (pH 6.8 at 25°C), 2% w/v SDS, 10% glycerol, 50 mM DTT, 0.01% w/v bromophenol blue or phenol red.

    Product Description

    Nonphosphorylated p70 S6 Kinase Control Cell Extracts: Total cell extracts from MCF-7 cells, prepared without treatment, serve as a negative control. Supplied in SDS Sample Buffer.
    Phosphorylated p70 S6 Kinase Control Cell Extracts: Total cell extracts from MCF-7 cells, prepared with insulin treatment, serve as a positive control. Supplied in SDS Sample Buffer.

    Background

    p70 S6 kinase is a mitogen activated Ser/Thr protein kinase that is required for cell growth and G1 cell cycle progression (1,2). p70 S6 kinase phosphorylates the S6 protein of the 40S ribosomal subunit and is involved in translational control of 5' oligopyrimidine tract mRNAs (1). A second isoform, p85 S6 kinase, is derived from the same gene and is identical to p70 S6 kinase except for 23 extra residues at the amino terminus, which encode a nuclear localizing signal (1). Both isoforms lie on a mitogen activated signaling pathway downstream of phosphoinositide-3 kinase (PI-3K) and the target of rapamycin, FRAP/mTOR, a pathway distinct from the Ras/MAP kinase cascade (1). The activity of p70 S6 kinase is controlled by multiple phosphorylation events located within the catalytic, linker and pseudosubstrate domains (1). Phosphorylation of Thr229 in the catalytic domain and Thr389 in the linker domain are most critical for kinase function (1). Phosphorylation of Thr389, however, most closely correlates with p70 kinase activity in vivo (3). Prior phosphorylation of Thr389 is required for the action of phosphoinositide 3-dependent protein kinase 1 (PDK1) on Thr229 (4,5). Phosphorylation of this site is stimulated by growth factors such as insulin, EGF and FGF, as well as by serum and some G-protein-coupled receptor ligands, and is blocked by wortmannin, LY294002 (PI-3K inhibitor) and rapamycin (FRAP/mTOR inhibitor) (1,6,7). Ser411, Thr421 and Ser424 lie within a Ser-Pro-rich region located in the pseudosubstrate region (1). Phosphorylation at these sites is thought to activate p70 S6 kinase via relief of pseudosubstrate suppression (1,2). Another LY294002 and rapamycin sensitive phosphorylation site, Ser371, is an in vitro substrate for mTOR and correlates well with the activity of a partially rapamycin resistant mutant p70 S6 kinase (8).
    No product specific background information is currently available for this product.
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.