Cell Signaling Technology

Product Pathways - Metabolism

Phospho-AMPKα (Thr172) Antibody #2531

alpha-2 chain   AMP-activated-kinase   AMPK   pampk   PRKA   PRKAA   PRKAA1   PRKAA2  

No. Size Price
2531L 300 µl ( 30 western blots ) ¥8,992.00 现货查询 购买询价 防伪查询
2531S 100 µl ( 10 western blots ) ¥3,960.00 现货查询 购买询价 防伪查询
2531 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 62 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,


Species predicted to react based on 100% sequence homology: Chicken, Bovine, Pig,

Specificity / Sensitivity

Phospho-AMPKalpha (Thr172) Antibody detects endogenous AMPKα only when phosphorylated at threonine 172. The antibody detects both α1 and α2 isoforms of the catalytic subunit, but it does not detect the regulatory beta or gamma subunits.

Phospho-AMPKα (Thr172)抗体可识别内源性的Thr172磷酸化的AMPKα。此抗体可识别催化亚基α1和α2,但不能识别调节亚基β或γ。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr172 of human AMPKα. Antibodies are purified by protein A and peptide affinity chromatography.


Western Blotting

Western Blotting

Western blot analysis of untreated and AICAR-treated C2C12 cell extracts using Phospho-AMPKα (Thr172) Antibody.

对未处理或AICAR处理的C2C12细胞系抽提液使用Phospho-AMPKα (Thr172) Antibody进行Western blot分析。


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).

AMP激活的蛋白激酶(AMPK)从酵母到动植物高度保守,在调节能量平衡上发挥关键作用(1)。AMPK是催化α亚基和调节β、γ亚基的异三聚体复合物,每个亚基由两个或三个独立基因编码(α1, 2;β1, 2;γ1, 2, 3)(2)。该激酶被细胞或环境应激时升高的AMP/ATP比率激活,如热休克、缺氧和缺血(1)。肿瘤抑制因子LKB1,与附属蛋白STRAD和MO25协同,磷酸化AMPKα活性环上的Thr172,此位点的磷酸化是AMPK活性所必需的(3-5)。AMPKα也可以被在Thr258和Ser485(α1,α2为Ser491)上磷酸化。这些磷酸化事件的上游激酶和生物学意义目前尚未阐清(6)。β1亚基的转录后修饰包括豆蔻酰化和多个位点的磷酸化(Ser24/25, Ser96, Ser101, Ser108, Ser182)(6,7)。β1亚基Ser108的磷酸化似乎是AMPK酶活性所必需,Ser24/25和Ser182的磷酸化影响AMPK的定位(7)。AMPKγ的若干突变已被确认,大部分都定位于推测的AMP/ATP结合位点(CBS或Bateman区域)。这些位点的突变导致AMPK活性的降低,导致心脏和骨骼肌中的糖原堆积(1,2)。越来越多的证据显示AMPK不仅调节脂肪酸和糖原代谢,也通过EF2和TSC2/mTOR通路调节蛋白质合成和细胞生长,通过eNOS/nNOS通路调节血流(1)。

  1. Hardie, D.G. (2004) J Cell Sci 117, 5479-87.
  2. Carling, D. (2004) Trends Biochem Sci 29, 18-24.
  3. Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87.
  4. Lizcano, J.M. et al. (2004) EMBO J 23, 833-43.
  5. Shaw, R.J. et al. (2004) Proc Natl Acad Sci USA 101, 3329-35.
  6. Woods, A. et al. (2003) J Biol Chem 278, 28434-42.
  7. Warden, S.M. et al. (2001) Biochem J 354, 275-83.
  8. Morales-Alamo, D. et al. (2013) J Appl Physiol 114, 566-77.
  9. Fullerton, M.D. et al. (2013) Nat Med 19, 1649-54.

Application References

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