The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Biological activityBiological Activity : Determined by a cytotoxicity assay using M1 cells. The expected ED50 for this effect is 0.5-1.0 µg/ml.
Endotoxin level< 0.100 Eu/µg
The gAcrp30 variant is a naturally occurring globular protein obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and named AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C long term.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ReconstitutionReconstitute to 1mg/ml using sterile water.
30 kDa adipocyte complement related protein
30 kDa adipocyte complement-related protein
Adipocyte C1q and collagen domain containing protein
Adipocyte complement related 30 kDa protein
Adipocyte complement related protein of 30 kDa
Adipocyte complement-related 30 kDa protein
adipocyte-specific secretory protein
adiponectin, C1Q and collagen domain containing
Adipose most abundant gene transcript 1
Adipose most abundant gene transcript 1 protein
Adipose specific collagen like factor
C1q and collagen domain-containing protein
Gelatin binding protein
Gelatin binding protein 28
FunctionImportant 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.
Tissue specificitySynthesized exclusively by adipocytes and secreted into plasma.
Involvement in diseaseDefects in ADIPOQ are the cause of adiponectin deficiency (ADPND) [MIM:612556]. ADPND results in very low concentrations of plasma adiponectin. Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance.
DomainThe C1q domain is commonly called the globular domain.
Post-translational modificationsHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-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. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation.