Cat. No.: DAA-001019
| Product Information | |
|---|---|
| Product Name | Total AMPKα Sandwich ELISA Kit |
| Species | Human; Mouse; Rat; Monkey |
| Description | Total AMPKα Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of AMPKα. An AMPKα Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, AMPKα (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a biotinylated AMPKα Rabbit Detection mAb is added to detect the captured phospho and nonphospho AMPKα protein. A HRP-linked streptavidin antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of total AMPKα. |
| Component | AMPKα Rabbit mAb Coated Microwells; AMPKα Rabbit Detection mAb; HRP-Linked Streptavidin (ELISA Formulated); Detection Antibody Diluent; HRP Diluent; TMB Substrate; STOP Solution; Sealing Tape; ELISA Wash Buffer (20X); ELISA Sample Diluent; Cell Lysis Buffer (10X) |
| Target Information | |
|---|---|
| Target Name | AAPK1; AAPK2 |
| UniProt No. | Q13131; P54646 |
| Target Description | AMP-activated protein kinase. The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia. 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. AMPKα is also phosphorylated at Thr258 and Ser485. The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated. The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. Phosphorylation at Ser108 of the β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization. Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites. Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle. 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. |
| Shipping & Storage | |
|---|---|
| Sipping | Shipping on dry ice. |
| Storage | Store at -20°C. Please refer to protocols. |
