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Upingbio
SKU:YP-Ab-14116-53UL
AMPKα1 Monoclonal Antibody
AMPKα1 Monoclonal Antibody
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- Reaction species: Human;Mouse;Rat;Monkey
- Gene Name: AAPK1
- Protein name: 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Immunogen: Purified recombinant fragment of human AMPKα1 expressed in E. Coli.
- Specificity: AMPKα1 Monoclonal Antibody detects endogenous levels of AMPKα1 protein.
- Composition: Ascitic fluid containing 0.03% sodium azide,0.5% BSA, 50%glycerol.
- Source: Monoclonal, Mouse
- Dilution ratio: Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/200 - 1/1000. Immunofluorescence: 1/200 - 1/1000. Flow cytometry: 1/200 - 1/400. ELISA: 1/10000. Not yet tested in other applications.
- Purification process: Affinity purification
- Storage: -20°C/1 year
- Other Names: PRKAA1;AMPK1;5'-AMP-activated protein kinase catalytic subunit alpha-1;AMPK subunit alpha-1;Acetyl-CoA carboxylase kinase;ACACA kinase
- Background: The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008],
- Function: catalytic activity:ATP + a protein = ADP + a phosphoprotein.,cofactor:Magnesium.,enzyme regulation:Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-174 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio.,function:Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic s
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