- 询价
- Cell Signaling Technology
- 4182
- USA
- 2025年08月31日
- W, IP
- Rabbit
- H,M,R,Mk
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- 详细信息
- 技术资料
- 抗体英文名：
AMPKβ1 Antibody
- 抗原：
synthetic peptide corresponding to the amino-terminal residues of human AMPKβ1
- 应用范围：
W, IP
- 宿主：
Rabbit
- 级别：
详见MSDS文件
- 库存：
大量
- 适应物种：
H,M,R,Mk
- 供应商：
CST
- 保质期：
详见说明书
- 是否单克隆：
2
- 保存条件：
-20°c
- 规格：
100 ul (10 western blots)/carrier free & custom formulation / quantity
| 规格： | 产品价格： | ￥请询价 | |
|---|---|---|---|
| 规格： | 100 ul (10 western blots) | 产品价格： | ￥请询价 |
| 规格： | carrier free & custom formulation / quantity | 产品价格： | ￥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting IP=Immunoprecipitation
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H M R Mk | Endogenous | 38 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | AMPKbeta1 Antibody detects endogenous levels of total AMPKβ1. The antibody does not cross-react with AMPKβ2. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal residues of human AMPKβ1. Antibodies are purified by protein A and peptide affinity chromatography. Western Blotting
Western blot analysis of extracts from HEK293, NIH/3T3, C6 and COS cells, using AMPKβ1 Antibody. IP
Immunuprecipitation of AMPKβ1 from untreated or oligomycin treated C2C12 cells using AMPKβ1 Antibody, followed by western blot analysis using AMPKβ1 Antibody (left) or Phospho-AMPKβ1 (Ser108) Antibody #4181 (right). |
| Background | 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).
|
| Application References |
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know ! |
| Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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