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Render Timestamp: 2024-12-23T11:34:07.497Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 15:28:07.157
Product last modified at: 2024-12-17T18:52:43.530Z
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PDP - Template Name: Cell Extracts
PDP - Template ID: *******b5396df
  1. Products /
  2. Experimental Controls /
  3. p70 S6 Kinase MCF7 Control Cell Extracts

p70 S6 Kinase MCF7 Control Cell Extracts #34499

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    Product Information

    Product Usage Information

    Boil for 3 minutes prior to use. Load 10 μl of phosphorylated and nonphosphorylated p70 S6 Kinase MCF7 Control Cell Extracts per lane.

    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 MCF7 cells, serum-starved overnight to serve as a negative control. Supplied in SDS Sample Buffer.

    Phosphorylated p70 S6 Kinase Control Cell Extracts: Total cell extracts from MCF7 cells, serum-starved overnight and treated 100 ng/ml hIGF-1 #8917 for 10 min to 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).

    Database Links

    UniProt ID: P23443


    Entrez-Gene Id: 6198


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