Product Name :
AMPK alpha 1 monoclonal antibody 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. Product :
Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide. Storage&Stability :
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Specificity :
Recognizes endogenous levels of AMPK alpha 1 protein. Immunogen :
KLH-conjugated synthetic peptide encompassing a sequence of human AMPK alpha 1. The exact sequence is proprietary. Conjugate :
Unconjugated Modification :
Unmodification

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  Western blot analysis of AMPK alpha 1 expression in Hela (A), 293T (B), NIH3T3 (C), PC12 (D) whole cell lysates.
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  Immunohistochemical analysis of AMPK alpha 1 staining in mouse colon formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.

Bioworld Biotech only provide peptides for our antibodies and do not provide additional peptide customization services.

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Price/Size :

USD 368/1mg/vial

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Tips: 

For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).

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Describe :

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (WB) and Immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or IHC performed with the neutralized antibody.

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Formula:

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.

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Storage:

The freeze-dried powder is more stable. For short time at 2-8°C. For long term storage store at -20°C. 

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Note :

This product is for research use only (RUO only). Not for use in diagnostic or therapeutic procedures.

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