Immunohistochemical analysis of Phospho-AMPK alpha-1 pThr172+AMPK alpha-2 pThr183 in paraffin-embedded human breast carcinoma using Phospho-AMPK alpha-1 pThr172+AMPK alpha-2 pThr183 polyclonal antibody (Product # PA5-36764) at a dilution of 1:100.
|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phosphopeptide derived from human AMPK alpha1 around the phosphorylation site of Threonine 183|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.2|
|Contains||0.05% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:200|
|Western Blot (WB)||1:500-1:1000|
* 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.
This antibody detects endogenous protein at a molecular weight of 63 kDa.
Purity is >95% by SDS-PAGE.
AMPK is a heterotrimeric complex comprising a catalytic alpha subunit and regulatory beta and gamma subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase, and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxymethylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPK alpha1 and AMPK alpha2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPK beta1 encodes a 271 amino acid protein and human AMPK beta2 encodes a 272 amino acid protein. The human AMPK gamma1 gene encodes a 331 amino acid protein. Human AMPK gamma2 and AMPK gamma3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.