antibody

AMP Activated Protein Kinase alpha1, phosphorylated (Ser485)/AMPKa2 (Ser491) (AMPK a1, AMPK a2)

A1475-05B

100 ul

polyclonal

domestic rabbit

nonconjugated

phosphorylated

AMP Activated Protein Kinase alpha1, phosphorylated (Ser485)/AMPKa2 (Ser491) (AMPK a1, AMPK a2)

rabbit

Pab

Phosphorylated

Antibodies

100 ul

IgG

AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals andplays a key role in the regulation of energy homeostasis 1). AMPK is a heterotrimeric complex composed of a catalytic a subunit and regulatory b and g subunits, each of which is encoded by two or three distinct genes a1, 2; b1, 2; g1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia and ischemia (1). Tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPK at Thr172 at the activation loop, and this phosphorylation is required for AMPK activation (3–5). AMPKa is also phosphorylated at Thr258 and Ser485 for a1; Ser491 for a2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The b1 subunit is posttranslationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the b1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKg 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 (1,2). 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 (1). Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilution: Western Blot: 1:1000. A band is detected at 62kD. Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot. Store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Hu Mk Mo Rt

Synthetic phosphopeptide corresponding to residues surrounding Ser491 of human AMPKa2.

Recognizes endogenous levels of human AMPKa1/a2 only when phosphorylated at serine 485 or serine 491. This antibody does not cross-react with other related proteins. Species Crossreactivity: Mouse, monkey and rat.

Purified by Protein A and peptide affinity chromatography

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol.

~0.1mg/ml

Product Type: Pab Isotype: IgG Host: rabbit Source: human Concentration: ~0.1mg/ml Form: Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol. Purity: Purified by Protein A and peptide affinity chromatography Immunogen: Synthetic phosphopeptide corresponding to residues surrounding Ser491 of human AMPKa2. Specificity: Recognizes endogenous levels of human AMPKa1/a2 only when phosphorylated at serine 485 or serine 491. This antibody does not cross-react with other related proteins. Species Crossreactivity: Mouse, monkey and rat. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

WB

-20°C

(1) Hardie, D.G. (2004) J. Cell Sci. 117, 5479-5487. (2) Carling, D. (2004) Trends Biochem. Sci. 29, 18–24. (3) Hawley, S.A. et al. (1996) J. Biol. Chem. 271, 27879–27887.(4) Lizcano, J.M. et al. (2004) EMBO J. 23, 833–843. (5) Shaw, R. et al. (2004) Proc. Natl. Acad. Sci. USA 101, 3329–3335. (6) Woods, A. et al. (2003) J. Biol. Chem. 278, 28434–28442. (7) Warden, S.M. et al. (2001) Biochem. J. 354, 275–283.

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