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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.

AMPKβ1/2 (57C12) Rabbit Antibody

INQUIRY

CAT. NO.: AMA-0085

Target Information
UniProt ID	Q9Y478

Product Details
Size	20 μL/100 μL
Reactivity	Human, Monkey, Mouse, Rat, Hamster
Host	Rabbit
Source/Isotype	Rabbit IgG
Storage	Store at -20°C.
Purification	Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence surrounding His233 residues of human AMPKβ1.

Usage
Application	WB, IHC, IF, F
Product Usage Information Dilution	Western Blotting (1:1000); Immunohistochemistry (1:100); Immunofluorescence (1:50); Flow Cytometry (1:100)
MW (Target)	30-38 kDa

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. 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). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia. 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. 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. The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. Phosphorylation at Ser108 of the β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization. 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. 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. 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.

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. 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). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia. 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. 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. The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. Phosphorylation at Ser108 of the β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization. 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. 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. 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.

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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.