Cat. # | Size | Qty. | Price |
---|---|---|---|
9957T | 1 Kit (6 x 20 microliters) |
|
Product Includes | Quantity | Applications | Reactivity | MW(kDa) | Isotype |
---|---|---|---|---|---|
Phospho-AMPKα (Thr172) (40H9) Rabbit mAb 2535 | 20 µl |
|
H M R Hm Mk Dm Sc | 62 | Rabbit IgG |
AMPKα (D5A2) Rabbit mAb 5831 | 20 µl |
|
H M R Mk B | 62 | Rabbit IgG |
Phospho-AMPKβ1 (Ser182) Antibody 4186 | 20 µl |
|
H M R Mk | 38 | Rabbit |
AMPKβ1/2 (57C12) Rabbit mAb 4150 | 20 µl |
|
H M R Hm Mk | 30, 38 | Rabbit IgG |
Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb 11818 | 20 µl |
|
H M R | 280 | Rabbit IgG |
Acetyl-CoA Carboxylase (C83B10) Rabbit mAb 3676 | 20 µl |
|
H M R Hm | 280 | Rabbit IgG |
Anti-rabbit IgG, HRP-linked Antibody 7074 | 100 µl |
|
Rab | Goat |
Product Information
Monoclonal state-specific antibod- ies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr172 of human AMPKα, and Ser79 of human ACC. Total monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg21 of human AMPKα, His233 of human AMPKß1, and Ser523 of human Acetyl-CoA Carboxylase α1. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser182 of human AMPKß1. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
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 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 and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation ot Ser24/25 and Ser182 affects AMPK localization (7). 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).
Acetyl-CoA carboxylase (ACC) catalyzes the pivotal step of the fatty acid synthesis pathway. The 265 kDa ACCα is the predominant isoform found in liver, adipocytes and mammary gland, while the 280 kDa ACCβ is the major isoform in skeletal muscle and heart (8). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (9). ACC is a potential target of anti-obesity drugs (10,11).
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