Active human Adiponectin peptide is a Synthetic blocking peptide. Suitable for BL.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application BL | Reactivity Reacts | Dilution info - | Notes - |
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Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.
ACDC, ACRP30, APM1, GBP28, ADIPOQ, Adiponectin, 30 kDa adipocyte complement-related protein, Adipocyte complement-related 30 kDa protein, Adipose most abundant gene transcript 1 protein, Gelatin-binding protein, apM-1
Active human Adiponectin peptide is a Synthetic blocking peptide. Suitable for BL.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS, 0.1% BSA
ab39918 is a crude synthetic peptide, purity range from 60-70%. The sequence is proprietary.
Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.
HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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