2535 Phospho-AMPKα (Thr172) (40H9) Rabbit mAb #2535

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产品详细参数如下>>>>

产品名称：Phospho-AMPKα (Thr172) (40H9) Rabbit mAb #2535
货号：2535
品牌：CST(cell signaling)
抗体来源：Rabbit
克隆类型： Monoclonal
规格：

No.	Size	Price
2535P	40 ul (4 western blots)	询价
2535S	100 ul (10 western blots)	询价
2535L	300 ul (30 western blots)	询价

抗体应用：

Applications	Reactivity	Sensitivity	MW (kDa)	Isotype
W IP IHC-P	H M R Hm Mk Dm Sc (C) (Z) (B) (Pg)	Endogenous	62	Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  Mk=Mon key  C=Chicken  Dm=D. melanogaster  Z=Zebrafish  B=Bovine  Pg=Pig  Sc=S. cerevisiae
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on sequence homology.
特异性/敏感度： Phospho-AMPKα (Thr172) (40H9) Rabbit mAb detects endogenous AMPKα only when phosphorylated at threonine 172. The antibody detects both α1 and α2 isoforms of the catalytic subunit, but does not detect the regulatory β or γ subunits.
来源及纯化方法： Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr172 of human AMPKα protein.
抗体背景：

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).

关键词：CST，抗体，一抗{byao_back}{byao_back2}

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