Product Name: AMPKa2 (374-382) pS377
Product Number: PE-04AHL80
Size:      $US
Peptide Name: AMPKa2 (374-382) pS377

Product Use: Services as a blocking peptide for use with the AMPKa2-pS377 rabbit polyclonal antibody (Cat. No.: AB-PK522) that is also available from Kinexus. This phosphopeptide may also be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the C-terminal half of the protein after the kinase catalytic domain. This is the major in vivo phosphorylation sites in AMPKa2. The effect of its phosphorylation is unclear.

Peptide Production Method: Solid-phase peptide synthesis

Peptide Origin: Homo sapiens

Peptide Sequence: IAD-pS-PKARC

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide
Peptide Modifications Other: Phosphorylated

Peptide Molecular Mass Calculated: 1110.18 Da

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Storage Stability: Not stable

Related Product 1: AMPKa2 - pS377 phosphosite-specific antibody (Cat. No.: AB-PK522)

Scientific Background: AMPKa2 (PRKAA2) is a protein-serine/threonine kinase of the CAMK group and CAMKL family. It is the catalytic subunit of AMP-activated protein kinase (AMPK),which is an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK 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. It also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Binding of AMP results in allosteric activation, inducing phosphorylation on T172 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39.It is also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. Defects in PRKAA2 are linked to Peutz-Jeghers Syndrome, which is a relatively rare autosomal dominant disease where benign polyps develop on the GI tract.