Cell Signaling Technology

Product Pathways - Metabolism

AMPKβ1 Antibody #12063

AMP-activated-kinase   AMPK   AMPK beta   beta-1 chain   PRKA   PRKAB   PRKAB1   PRKAB2  

No. Size Price
12063S 100 µl ( 10 western blots ) ¥3,250.00 现货查询 购买询价 防伪查询
12063 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Monkey, Endogenous 38 Rabbit
IP 1:50

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

AMPKβ1 Antibody detects endogenous levels of total AMPKβ1 protein. The antibody does not cross-react with AMPKβ2.

AMPKβ1 Antibody能够检测内源性的AMPKβ1总蛋白水平。该抗体不与AMPKβ2发生交叉反应

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal residues of human AMPKβ1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

该多克隆抗体是由合成的人源AMPKβ1蛋白N末端肽段免疫动物而制备的。抗体由protein A和肽亲和层析技术纯化。

Western Blotting

Western Blotting

Western blot analysis of extracts from 293 and COS-7 cells using AMPKβ1 Antibody.

Western blot 检测293 和COS-7细胞提取物,使用抗体为AMPKβ1 Antibody。



Immunoprecipitation of AMPKβ1 from COS-7 cell extracts using Normal Rabbit IgG #2729 (lane 2) or AMPKβ1 Antibody (lane 1). Lane 3 is 10% input. Western blot analysis was performed using AMPKβ1 Antibody (upper) or AMPKβ2 Antibody #4148 (lower).

免疫沉淀方法检测COS-7 细胞提取物AMPKβ1蛋白,使用Normal Rabbit IgG #2729 (泳道2) 或 AMPKβ1 Antibody (泳道1)。泳道3为10%对照。Western blot方法检测,使用AMPKβ1 Antibody (上图) 或 AMPKβ2 Antibody #4148 (下图)


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依赖的蛋白激酶(AMPK)从酵母到植物和动物都高度保守,在调节能量平衡方面起关键作用(1)。AMPK蛋白以一种异源三聚体复合物的形式存在,由一个α-催化亚基、一个β-调节亚基和一个γ-调节亚基组成,每个亚基被两到三个不同基因编码(α1,β1,γ1,2,3)(2)。该激酶会被因细胞和环境压力引起的AMP/ ATP比值升高而激活,如热休克,缺氧和缺血(1)。肿瘤抑制因子LKB1与辅助蛋白STRAD和MO25一同将位于AMPKα活化环的Thr172磷酸化,该位点的磷酸化是AMPK激酶活性所必需的(3-5)。 AMPKα的Thr258和Ser485(α1是Ser485,α2是Ser491)也被磷酸化。上游激酶以及这些磷酸化事件的生物学意义尚未被阐明(6)。β1亚基是被翻译后修饰的,如肉豆蔻酰化和多位点磷酸化包括Ser24/25,Ser96,Ser101,Ser108和Ser182(6,7)。β1亚基Ser108磷酸化似乎是需要AMPK激酶活性的,而Ser24/25和Ser182磷酸化会影响AMPK定位(7)。已确定了几个AMPKγ亚基的突变,其中大部分是位于假定AMP/ ATP结合位点(CBS或贝特曼域)。在这些位点的突变导致AMPK活性降低,引起心脏或骨骼肌内糖原积累(1,2)。越来越多的证据表明,AMPK不仅调节脂肪酸和糖原代谢,也通过EF2和TSC2/mTOR途径调节蛋白质合成和细胞生长,另外还通过eNOS / nNOS调节血流量(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.

Application References

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