The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human AMPK that contains threonine 172. The sequence is conserved in human, mouse and rat.
Conjugate
Unconjugated
Form
Liquid
Purification
Antigen affinity chromatography
Storage buffer
Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol
Contains
0.05% sodium azide
Storage Conditions
-20°C
Tested Applications
Dilution *
Flow Cytometry (Flow)
3-5 µg x 10^6 cells
Immunocytochemistry (ICC)
1 µg/ml
Immunofluorescence (IF)
1 µg/ml
Immunohistochemistry (Paraffin) (IHC (P))
1:10-1:50
Western Blot (WB)
Assay Dependent
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Background/Target Information
The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.
原厂资料：
注意事项：
For Research Use Only. Not for use in diagnostic procedures.
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