- 询价
- Cell Signaling Technology
- 5831
- USA
- 2025年07月16日
- W, IP
- H,M,R,Mk,B
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- 详细信息
- 文献和实验
- 技术资料
- 级别：
详见MSDS文件
- 抗原：
synthetic peptide corresponding to residues surrounding Arg21 of human AMPKα
- 供应商：
CST
- 是否单克隆：
单克隆
- 抗体英文名：
AMPKα (D5A2) Rabbit mAb
- 保质期：
详见说明书
- 保存条件：
-20°c
- 应用范围：
W, IP
- 适应物种：
H,M,R,Mk,B
- 库存：
大量
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 B=Bovine
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) | Isotype |
|---|---|---|---|---|
| W IP | H M R Mk B | Endogenous | 62 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | AMPKα (D5A2) Rabbit mAb detects endogenous levels of total AMPKα protein. |
| Source / Purification | Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg21 of human AMPKα. Western Blotting
Western blot analysis of extracts from HeLa, K-562, C6, and Neuro-2a cells using AMPKα (D5A2) Rabbit mAb. |
| 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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文献和实验Immunofluorescence: Rabbit Anti-Murine RELMα
for 25 minutes. 3. Incubate the tissue section with blocking buffer for 20 minutes. 4. Incubate the tissue section overnight at 4?C with Rabbit Anti-Murine RELMα at 4.0 ng/mL in 1X PBS with 0.01% Triton-X and 0.5% BSA. Wash the slide
Isolation and Purification of Rabbit Osteoclasts
rabbit osteoclasts on resorbable substrates in vitro are an ideal model of osteoclast behaviour in vivo, and for some studies may be preferable to osteoclast-like cells generated in vitro from bone marrow cultures or from human peripheral blood
Assaying Phospholipase A2 Activity
Mammalian cells contain many structurally and functionally diverse phospholipases A2 (PLA2 ) that catalyze the hydrolysis of sn-2 fatty acid from membrane phospholipid. Assays are described for measuring the activity of Group IVA cytosolic
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