p-AMPKα1 (S487) pAb

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Catalogue No : BS4010

Alternative Name for p-AMPKα1 (S487) pAb
Host   Reactivity Size Application stock price cart
Rabbit H,M,R 100μg WB IHC 298.00
Contact information

Email:shdiahds@163.com
Phone:+1-909-839-7620
Fax:+1-909-839-7620

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Product

1 mg/ml in Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.2.

Molecular Weight

~65.0 kDa

Purification & Purity

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Specificity

p-AMPKα1 (S487) pAb detects endogenous levels of p-AMPKα1 protein.

Applications (Recommended Dilutions)

WB: 1:500~1:1000 IHC: 1:50~1:200

Western Blot(WB)

Western blot (WB) analysis of p-AMPKα1 (S487) pAb in extracts from hela ,PC12 and Raw264.7 cells.

Immunohistochemistry (IHC)

Immunohistochemistry (IHC) analyzes of p-AMPKα1 (S487) pAb in paraffin-embedded human colon carcinoma tissue.

Storage&Stability

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Background

AMPK (for 5'-AMP-activated protein kinase) is a heterotrimeric complex comprising a catalytic α subunit and regulatory β and γ 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 AMPKα1 and AMPKα2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKβ1 encodes a 271 amino acid protein and human AMPKβ2 encodes a 272 amino acid protein. The human AMPKγ1 gene encodes a 331 amino acid protein. Human AMPKγ2 and AMPKγ3, 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.