antibody

Phospho-AMPKbeta1-S108

MBS9126886

0.05 mL

235 USD

polyclonal

rabbit

nonconjugated

Antibody

Phospho-AMPKbeta1-S108

[AMPKbeta1-S108]

[Phospho-AMPKb1-S108, AMPK; HAMPKb]

[5'-AMP-activated protein kinase subunit beta-1; 5'-AMP-activated protein kinase subunit beta-1; 5'-AMP-activated protein kinase subunit beta-1; AMPKb; AMPK beta 1; AMPK beta -1 chain; AMPK subunit beta-1; AMP-activated protein kinase beta subunit; 5'-AMP-activated protein kinase beta-1 subunit; protein kinase, AMP-activated, noncatalytic, beta-1; protein kinase, AMP-activated, beta 1 non-catalytic subunit]

[PRKAB1]

[PRKAB1; PRKAB1; AMPK; HAMPKb; AMPK; AMPK subunit beta-1; AMPKb]

AAKB1_HUMAN

Polyclonal

IgG

Rabbit

Human

270

Affinity purification

Store at -20°C. Avoid freeze / thaw cycles.

Western Blot (WB)

WB 1:500-1:2000

Western Blot (WB)

Immunogen: A phospho specific peptide corresponding to residues surrounding S108 of human AMPKbeta1. Calculated MW: 30kDa. Observed MW: 40kDa

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Phosphorylation

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.

14194425

Q9Y478.4

Q9Y478

AMPK Signaling Pathway (198868); AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Activation Of PPARGC1A (PGC-1alpha) By Phosphorylation Pathway (1127496); Adipocytokine Signaling Pathway (83093); Adipocytokine Signaling Pathway (505); Circadian Rhythm Pathway (83084); Circadian Rhythm Pathway (495); Direct P53 Effectors Pathway (137939); Energy Metabolism Pathway (198907)

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008]

AMPKB1: a non-catalytic subunit of AMPK, a conserved kinase of the CAMKL family. AMPK is an energy-sensing protein that plays a key role in regulating cellular energy homeostasis. Environmental stress, such as heat shock, nutrient deprivation, hypoxia and ischemia, indirectly activate AMPK by the depletion of cellular ATP and the concomitant rise of ADP and AMP levels. Allosteric activation is achieved primarily by rising ADP levels, and not solely by AMP levels as previously thought. Activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton, probably by indirectly activating myosin. AMPK is a heterotrimer of an alpha catalytic subunit (AMPKA1 or -2), a beta (AMPKB1 or -2) and a gamma non-catalytic subunit (AMPKG1, -2 or -3). Different possible combinations of subunits give rise to 12 different holoenzymes. Beta subunits act as scaffolds on which the AMPK complex assembles, via its C-terminus that bridges alpha and gamma subunits. AMPK-beta1 or -beta2 subunits are required for assembling of AMPK heterotrimers and are important for regulating enzyme activity and cellular localization. AMPK beta1beta2 null mouse muscles reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise. Phosphorylation by ULK1 and ULK2 inhibits AMPK activity. Hematopoietic AMPKB1 reduces mouse adipose tissue macrophage inflammation and insulin resistance in obesity. Protein type: Protein kinase, regulatory subunit; Autophagy. Chromosomal Location of Human Ortholog: 12q24.1-q24.3. Cellular Component: nucleus; cytosol; AMP-activated protein kinase complex. Molecular Function: AMP-activated protein kinase activity; protein binding; protein kinase binding; protein kinase activity. Biological Process: mitochondrion organization and biogenesis; protein heterooligomerization; organelle organization and biogenesis; insulin receptor signaling pathway; cell cycle arrest; signal transduction; regulation of protein kinase activity; protein amino acid phosphorylation; fatty acid biosynthetic process

0.05 mL

235 USD

0.1 mL

350

0.2 mL

525