p70[S6K] Pure 16/p70[s6k] 50ug

S6 Kinase β2 (pT421/S424)

Mouse IgG1

Rat p70 [S6K] aa. 2-121

Increased protein synthesis, an obligatory step in cell proliferation, is regulated by the phosphorylation of a number of translational components, such as ribosomal protein S6.  p70 S6 Kinase (p70 [S6K]), a cytosolic kinase that is primarily responsible for S6 phosphorylation, belongs to a family of at least six S6 kinases.  p70 [S6K] and p85 [S6K] are two isoforms of the same kinase.  Although they are encoded by the same gene, p80 [S6K] contains a 23 amino acid N-terminal extension that serves as a nuclear localization sequence.  These kinases are located in a p21 ras-independent signaling pathway and are regulated by Ser/Thr phosphorylation in response to mitogenic stimulation.  Activation of p70 [S6K] requires sequential phosphorylations within the autoinhibitory domain and at Thr 389.  p70 [S6K] associates with PDK-1 and PKCζ to form a possible PI3-K signaling complex.  The immunosuppressive agent rapamycin forms an intracellular complex with FKBP12 and FRAP (RAFT1) that inhibits phosphorylation of p70 [S6K] at Thr 389 and, in turn, prevents enzyme activation.  Thus, p70 [S6K] is an important regulator of cell proliferation and a potential target of agents that modify the immune and proliferative responses.  p70 [S6K] has been reported to be observable migrating within a range of 60-70 kD by western blotting.

16/p70[s6k] Increased protein synthesis, an obligatory step in cell proliferation, is regulated by the phosphorylation of a number of translational components, such as ribosomal protein S6.  p70 S6 Kinase (p70 [S6K]), a cytosolic kinase that is primarily responsible for S6 phosphorylation, belongs to a family of at least six S6 kinases.  p70 [S6K] and p85 [S6K] are two isoforms of the same kinase.  Although they are encoded by the same gene, p80 [S6K] contains a 23 amino acid N-terminal extension that serves as a nuclear localization sequence.  These kinases are located in a p21 ras-independent signaling pathway and are regulated by Ser/Thr phosphorylation in response to mitogenic stimulation.  Activation of p70 [S6K] requires sequential phosphorylations within the autoinhibitory domain and at Thr 389.  p70 [S6K] associates with PDK-1 and PKCζ to form a possible PI3-K signaling complex.  The immunosuppressive agent rapamycin forms an intracellular complex with FKBP12 and FRAP (RAFT1) that inhibits phosphorylation of p70 [S6K] at Thr 389 and, in turn, prevents enzyme activation.  Thus, p70 [S6K] is an important regulator of cell proliferation and a potential target of agents that modify the immune and proliferative responses.  p70 [S6K] has been reported to be observable migrating within a range of 60-70 kD by western blotting.

Mouse IgG1

克隆 16/p70[s6k] (RUO)

250 µg/ml

Western blot (Routinely Tested), Immunofluorescence (Tested During Development)

Rat (QC Testing), Human, Mouse (Tested in Development)

S6 Kinase β2 (pT421/S424)

p70 S6 Kinase

Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

研发参考(4) 1. Brennan P, Babbage JW, Thomas G, Cantrell D. p70(s6k) integrates phosphatidylinositol 3-kinase and rapamycin-regulated signals for E2F regulation in T lymphocytes. Mol Biol Cell. 1999; 19(7):4729-4738. (Biology). 2. Johanson SO, Naccache PA, Crouch MF. A p85 subunit-independent p110alpha PI 3-kinase colocalizes with p70 S6 kinase on actin stress fibers and regulates thrombin-stimulated stress fiber formation in swiss 3T3 cells. Exp Cell Res. 1999; 10(1):223-233. (Biology). 3. Ming XF, Burgering BM, Wennstrom S. Activation of p70/p85 S6 kinase by a pathway independent of p21ras. Nature. 1994; 371(6496):426-429. (Biology). 4. Romanelli A, Martin KA, Toker A, Blenis J. p70 S6 kinase is regulated by protein kinase Czeta and participates in a phosphoinositide 3-kinase-regulated signalling complex. Mol Cell Biol. 1999; 19(4):2921-2928. (Biology).