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ADIPONECTIN ANTIBODIES > ADIPONECTIN POLYCLONAL ANTIBODY PA1-12844
Anti-Adiponectin Polyclonal Antibody
Printable Datasheet
Synonyms:
ACDC, ACRP30, APM-1, APM1, GBP28, ADPIOQ
Entrez Gene ID:
(Human) 9370, (Murine) 11450, (Rat) 246253
UniProt ID:
Q15848
| Details | |
| Host / Isotype: | Rabbit / IgG |
| Class: | Polyclonal |
| Type: | Antibody |
| Species Reactivity: | Human (Hu) Murine (Ms) Rat (Rt) |
| Immunogen: | Synthetic peptide corresponding to 15 residues from near the N-terminus of human adiponectin. |
| Ordering Information | ||||
| Pierce Anti-Adiponectin Polyclonal Antibody | ||||
| Product Number | Pkg. Size | Price | Purchase | |
| PA1-12844 | 100 µg | $368.00 | ||
| Storage: | -20º C, Avoid Freeze/Thaw Cycles |
| Form: | 100 µg of antibody (1 mg/ml) in PBS with 0.02% sodium azide. |
| Applications | Dilution |
| Immunohistochemistry (IHC) | Assay Dependent |
| Western Blot (WB) | 1-4 ug/ml |
| Product Specific Information |
| PA1-12844 detects Adiponectin in human, mouse and rat samples. PA1-12844 has been successfully used in western blot and immunohistochemistry procedures. The PA1-12844 immunogen is a synthetic peptide corresponding to 15 residues from near the N-terminus of human adiponectin. |
| General Information |
| Adiponectin (also known as 30-kDa adipocyte complement-related protein; Acrp30) is a hormone secreted by adipocytes that acts as an antidiabetic and anti-atherogenic adipokine. Levels of adiponectin in the blood are decreased under conditions of obesity, insulin resistance and type 2 diabetes. Administration of adiponectin causes glucose-lowering effects and ameliorates insulin resistance in mice. Conversely, adiponectin-deficient mice exhibit insulin resistance and diabetes. This insulin-sensitizing effect of adiponectin seems to be mediated by an increase in fatty-acid oxidation through activation of AMP kinase and PPAR- . Here we report the cloning of complementary DNAs encoding adiponectin receptors 1 and 2 (AdipoR1 and AdipoR2) by expression cloning. AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. These two adiponectin receptors are predicted to contain seven transmembrane domains, but are structurally and functionally distinct from G-protein-coupled receptors. Expression of AdipoR1/R2 or suppression of AdipoR1/R2 expression by small-interfering RNA supports our conclusion that they serve as receptors for globular and full-length adiponectin, and that they mediate increased AMP kinase and PPAR- ligand activities, as well as fatty-acid oxidation and glucose uptake by adiponectin. |
(This product is for In Vitro experimental use only.)
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