Description
Product Usage Information
Western Blotting: 1:1000
Immunohistochemistry (Paraffin): 1:100
Immunofluorescence (Immunocytochemistry): 1:50
Flow Cytometry (Fixed/Permeabilized): 1:100
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody.
Protocol
Available protocols: Western Blotting, Immunohistochemistry (Paraffin), Immunofluorescence (Immunocytochemistry), Flow Cytometry (Fixed/Permeabilized)
Specificity / Sensitivity
AMPK beta1/2 (57C12) Rabbit Monoclonal Antibody detects endogenous levels of both total AMPKβ1 and β2 proteins. This antibody does not cross-react with other related proteins.
Species Reactivity: Human, Mouse, Rat, Hamster, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence surrounding His233 residues of human AMPKβ1.
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 AMPK activation, 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). AMPKbeta1 and AMPKbeta2 share approximately 70% sequence homology. Both isoforms contribute equally to AMPK activity. AMPKβ1 is predominantly expressed in the liver and brain, and shows minimal expression in kidney and skeletal muscle. In comparison, AMPKβ2 is highly expressed in skeletal muscle, and is expressed at low levels in kidney, liver, and lung.
Alternate Names
5'-AMP-activated protein kinase beta-1 subunit; 5'-AMP-activated protein kinase subunit beta-1; 5'-AMP-activated protein kinase subunit beta-2; 5'-AMP-activated protein kinase, beta-2 subunit; AAKB1; AAKB2; AMP-activated protein kinase beta 2 non-catalytic subunit; AMP-activated protein kinase beta subunit; AMPK; AMPK beta -1 chain; AMPK beta 1; AMPK beta 2; AMPK beta-2 chain; AMPK subunit beta-1; AMPK subunit beta-2; AMPKb; AMPKB1; AMPKB2; HAMPKb; MGC17785; MGC61468; PRKAB1; PRKAB2; protein kinase AMP-activated non-catalytic subunit beta 1; protein kinase AMP-activated non-catalytic subunit beta 2; protein kinase, AMP-activated, beta 1 non-catalytic subunit; protein kinase, AMP-activated, beta 2 non-catalytic subunit; protein kinase, AMP-activated, noncatalytic, beta-1
