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Phospho-Drosophila p70 S6 Kina

se (Thr398) Antibody
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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年12月31日
  • W
  • Rabbit
  • H,Dm
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名

      Phospho-Drosophila p70 S6 Kinase (Thr398) Antibody

    • 抗原

      synthetic phosphopeptide corresponding to residues surrounding Thr398 of Drosophila p70 S6 kinase

    • 应用范围

      W

    • 宿主

      Rabbit

    • 库存

      大量

    • 适应物种

      H,Dm

    • 供应商

      CST

    • 级别

      详见MSDS文件

    • 保质期

      详见说明书

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting
    Reactivity Key:  H=Human  Dm=D. melanogaster
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W H Dm Endogenous 70 Rabbit
    Protocols
    Specificity / Sensitivity

    Phospho-Drosophila p70 S6 Kinase (Thr398) Antibody detects endogenous levels of Drosophila p70 S6 kinase only when phosphorylated at threonine 398. The antibody will also recognize human p70 S6 Kinase when phosphorylated at threonine 389.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr398 of Drosophila p70 S6 kinase. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from Drosophila S2 cells and Human MCF-7 cells, using Phospho-Drosophila p70 S6 Kinase (Thr398) Antibody (upper), Phospho-p70 S6 Kinase (Thr389) Antibody #9205, which recognizes the human, mouse and rat protein (middle), or Akt Antibody #9272 (lower). Serum-starved S2 cells were untreated or treated with EGF (100 ng/ml, 30min) #9908. Serum-starved MCF-7 cells were untreated or treated with IGF-1 (50 ng/ml) in the presence or absence of LY294002 (10 uM) #9901.

    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).

    Drosophila p70 S6 kinase (dS6K) is a critical regulator of cell growth, but this effect is independent of Akt and PI-3K signaling (9,10). However, insulin-induced activation and phosphorylation of dS6K at Thr398 is dependent on PI-3K, mTOR, and Akt (11,12).

    1. Pullen, N. and Thomas, G. (1997) FEBS Lett. 410, 78-82.
    2. Dufner, A. and Thomas, G. (1999) Exp. Cell Res. 253, 100-109.
    3. Weng, Q.P. et al. (1998) J. Biol. Chem. 273, 16621-16629.
    4. Pullen, N. et al. (1998) Science 279, 707-710.
    5. Alessi, D.R. et al. (1998) Curr. Biol. 8, 69-81.
    6. Polakiewicz, R.D. et al. (1998) J. Biol. Chem. 273, 23534-23541.
    7. Fingar, D.C. et al. (2002) Genes Dev. 16, 1472-1487.
    8. Saitoh, M. et al. (2002) J. Biol. Chem. 277, 20104-20112.
    9. Montagne, J. et al. (1999) Science 285, 2126-2129.
    10. Radimerski, T. et al. (2002) Nat. Cell Biol. 4, 251-255.
    11. Lizcano, J. M. et al. (2003) Biochem. J. 374, 297-306.
    12. Miron, M. et al. (2003) Mol. Cell. Biol. 23, 9117-9126.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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    图标文献和实验
    相关实验
    • Using Phospho‐Motif Antibodies to Determine Kinase Substrates

      comprising both the phosphorylated residue and the surrounding residues that determine kinase specificity, with degenerate residues taking up the remaining positions. Currently, several categories of phospho?motif antibody are commercially available

    • ERK-MAP Kinase Signaling in the Cytoplasm

      . We describe two complementary methods for quantitatively measuring ERK activity toward the cytoplasmic p90 ribosomal S6 kinase (RSK). The first method is a straightforward immunoblot of endogenous ERK and RSK phosphoepitopes using phospho-specific antibodies. Infrared

    • Measurement of Phosphoinositide 3-Kinase Activity

      only PtdIns as a substrate (e.g., mammalian PtdIns 3-kinase and yeast Vps34p) ( 1 ). Generally, PI 3 kinases are now regarded as an important intracellular signal upstream of a variety of biochemical (e.g., activation of Akt/protein kinase B and/or p70

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