| 货号 | 3827S |
| 反应种属 | Human/Mouse/Rat/Monkey |
| 来源宿主 | Rabbit |
| 应用 | W |
| 目标/特异性 | Phospho-PKM2 (Tyr105) Antibody detects endogenous levels of PKM2 protein only when phosphorylated at Tyr105. This antibody may slightly cross react with PKM1 phosphorylated at the equivalent site. |
| 使用方法 | WB(1:1000) |
| 供应商 | CST |
| 背景 | Pyruvate kinase, a glycolytic enzyme, catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2), an alternatively-spliced variant of M1, is expressed during embryonic development (1). Studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors (Warburg effect) (1). When the M2 isoform is switched to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased in cancer cells (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies show that the oncogenic forms of FGFR1 directly phosphorylate Tyr105 of PKM2 and thereby inhibit the formation of active tetrameric PKM2 (4). A PKM2 mutant found in cancer cells, in which Tyr105 is replaced by phenylalanine, leads to reduced cell proliferation in hypoxia and tumor growth in xenografts in nude mice (4). These findings suggest that the phosphorylation at Tyr105 is a critical switch for the metabolism in cancer cells that promotes tumor growth (4). |
| 存放说明 | -20C |
| 计算分子量 | 60 |
Western blot analysis of extracts from A549 and DU 145 cells using Phospho-PKM2 (Tyr105) Antibody (upper) or PKM2 Antibody #3198 (lower). 对A549细胞和DU 145细胞抽提液，使用Phospho-PKM2 (Tyr105)抗体（上图）或PKM2抗体#3198（下图）进行Western blot分析。 | |
GST-PKM2 wild-type or the Tyr105Phe mutant was incubated in an in vitro kinase assay in the presence or absence of active FGFR1. Western blot analysis was performed using Phospho-PKM2 (Tyr105) Antibody and a phospho-Tyr antibody. The data demonstrate the specificity of the Phospho-PKM2 (Tyr105) Antibody and that the Tyr105Phe mutation abolishes PKM2 phosphorylation at Tyr105 by FGFR1 in vitro. (Adapted from Hitosugi, T. et al., 2009). GST-PKM2野生型或Tyr105Phe突变体在体外孵育以在活性FGFR1存在或不存在时进行激酶测试。使用Phospho-PKM2 (Tyr105)抗体和phospho-Tyr抗体进行Western blot分析。数据显示了Phospho-PKM2 (Tyr105)的特异性，Tyr105Phe突变消除了PKM2被FGFR1在体外对其Tyr105的磷酸化。（修改自Hitosugi, T. et al., 2009） | |
Western blot analysis of NCI-H1299 cells using Phospho-PKM2 (Tyr105) Antibody, total PKM2 Antibody #3198, total FGFR1 antibody, phospho-Tyr antibody, and β-actin antibody. The data demonstrate that inhibition of FGFR1 by TKI258 treatment in NCI-H1299 cells results in decreased Tyr105 phosphorylation of endogenous PKM2. (Adapted from Hitosugi, T. et al., 2009). 使用Phospho-PKM2 (Tyr105)抗体，总PKM2抗体#3198，总FGFR1抗体，phospho-Tyr抗体和β-actin抗体对NCI-H1299细胞进行Western blot分析。数据显示TKI258处理NCI-H1299细胞抑制FGFR1，导致内源性PKM2 Tyr105的磷酸化降低。（修改自Hitosugi, T. et al., 2009） |
