A4611
AMPK (α1/β2/γ1), active, His tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
AMPKG, MGC33776, MGC57364, MGC61468, MGC8666, PRKAA1, PRKAB2, PRKAG1
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About This Item
UNSPSC Code:
51111800
NACRES:
NA.32
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
297-401 nmol/min·mg
mol wt
A1 subunit ~68 kDa
B2 subunit ~36 kDa
G1 subunit ~40 kDa
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRKAA1(5562), PRKAB2(5565), PRKAG1(5571)
Biochem/physiol Actions
AMPK (A1/B2/G1) is a member of the AMPK family which are heterotrimeric proteins consisting of an α catalytic subunit, and non-catalytic β and γ subunits. AMPKs are an important energy-sensing enzyme group in the cells that monitor energy status particularly in response to stress. AMPKs regulate fatty acid and cholesterol synthesis by regulating the key rate-limiting enzymes acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA reductase. The β subunit may be a positive regulator of AMPK activity and is highly expressed in skeletal muscle.
Physical form
Supplied in 50 mM Sodium Phosphate, pH 7.0, with 150 mM imidazole, 0.1 mM PMSF, 0.2 mM DTT, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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C Thornton et al.
The Journal of biological chemistry, 273(20), 12443-12450 (1998-06-20)
The AMP-activated protein kinase (AMPK) is a member of a growing family of related kinases, including the SNF1 complex in yeast, which respond to nutritional stress. AMPK is a heterotrimeric complex of a catalytic subunit (alpha) and two regulatory subunits
B Viollet et al.
Biochemical Society transactions, 31(Pt 1), 216-219 (2003-01-28)
AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid metabolism. To understand better the physiological role of the catalytic AMPK subunit isoforms, we generated two knockout mouse models with the alpha1 (AMPK alpha 1(-/-)) and
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