| 货号 | 8208S |
| 描述 | PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CSTs product offering based upon superior performance in specified applications.CST的磷酸化套装主要用于检测蛋白激活状态。每套都提供了所需的总蛋白抗体和活化态抗体。套装中的抗体全部选自CST公司产品中表现最好的抗体。 |
| 供应商 | CST |
| 背景 | AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1). |
| 存放说明 | -20C |
| 参考文献 | Hardie, D.G. (2004) J Cell Sci 117, 5479-87. Carling, D. (2004) Trends Biochem Sci 29, 18-24. Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87. Lizcano, J.M. et al. (2004) EMBO J 23, 833-43. Shaw, R.J. et al. (2004) Proc Natl Acad Sci USA 101, 3329-35. Woods, A. et al. (2003) J Biol Chem 278, 28434-42. Warden, S.M. et al. (2001) Biochem J 354, 275-83. |
Western blot analysis of extracts from C2C12 cells, untreated or oligomycin-treated (0.5 µM), using Phospho-AMPKα (Thr172) (40H9) Rabbit mAb (upper) or AMPKα Antibody #2532 (lower). | |
Immunohistochemical analysis of paraffin-embedded NCI-H228 cell pellets, control (left) or phenformin-treated (right), using Phospho-AMPKalpha (T172) (40H9) Rabbit mAb. | |
Western blot analysis of extracts from HeLa, K-562, C6, and Neuro-2a cells using AMPKα (D63G4) Rabbit mAb. |
