P70 S6 Kinase beta Rabbit Recombinant mAb
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使用信息
| 抗体应用 | wb,ELISA | ||
|---|---|---|---|
| 稀释比例 |
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| 反应性 | Human Mouse Rat | ||
| MW (kDa) | 53kDa | ||
| 抗体类型 | Rabbit | ||
| 浓度 | 1mg/ml | ||
| 储存液配方 | 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. | ||
| 储存条件 (自收到货起) |
Store at –20°C. |
生物描述
| 特异性 | P70 S6 Kinase beta Rabbit Recombinant mAb detects endogenous levels of total P70 S6 Kinase beta |
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| 背景 | Cytokines often deliver simultaneous, yet distinct, cell growth and cell survival signals. The 70-kDa ribosomal protein S6 kinase (p70S6K) is known to regulate cell growth by inducing protein synthesis components. The p70 S6 kinase α (p70α, also named S6K1) is an insulin/mitogen-activated protein kinase in mammalian cells, whose major known substrate is the 40 S ribosomal subunit protein S6. p70 S6 kinase β (p70β, also named S6K2), another isoform of p70 S6 kinase, is a highly homologous amino acid sequence to that of p70α. There are two potential isoforms of the protein, p70 S6 kinase β1 and β2 (p70β1 and p70β2, also named S6K2βI and S6K2βII, respectively). p70β may be regulated through the multisite phosphorylation mechanism which is similar to that for p70α. Possible phosphorylation sites of p70β are well conserved: Thr241, Ser383 and Thr401 in p70β1 correspond to Thr252, Ser394 and Thr412 in p70α1, respectively. while p70β2 exhibits significantly different sensitivity against inhibition by rapamycin and wortmannin compared to p70α. As for the cellular location, p70β1 is mostly accumulated in the nucleus, whereas p70β2 were dispersed in the cytoplasm including nucleoplasm. The expression of p70β proteins is tightly regulated at the post-transcriptional level in each tissue: p70β1 is expressed in limited tissues. It is S6K2 (p70β), but not S6K1 (p70α), that is phosphorylated in vitro as well as in vivo by protein kinase C (PKC). The site of phosphorylation was identified as S486 in p54 S6K2 (S486 in p56 S6K2), located within the C-terminal NLS. While phosphorylation of this site did not affect the activity of S6K2, it impaired the function of the NLS leading to cytoplasmic accumulation of the kinase upon cell stimulation with PKC agonists such as PMA. All PKC isoforms were capable of phosphorylating S6K2, with PKCδ appearing to be the most efficient in vitro. However, this specificity seemed to disappear in vivo with all PKCs being equally potent. In addition to phosphorylation events, S6K2 is also the target of ubiquitination and of acetylation on a lysine residue close to the C-terminal PDZ binding motif. The latter modification does not impact on S6K2 kinase activity or sub-cellular localization but increases the stability of this kinase. S6K2 is expressed at various levels in different mouse and human tissues, and its expression levels often inversely correlate with those of S6K1. In Humans, S6K2 expression was found in all tissues with the exception of the neuropil, the peripheral nervous system, and adipocytes. However, expression levels between organs vary considerably, with highest levels found in the gastrointestinal tract, the central nervous system and the lung. In contrast, most mesenchymal cells stain weakly for S6K2. Although S6K2 is detected in normal tissues, its expression levels are often very low compared to those found in corresponding tumor samples. |
实验方法
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