The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 1 - 2 µg/ml. Predicted molecular weight: 30 kDa.
Use a concentration of 10 - 20 µg/ml.
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.
30 kDa adipocyte complement related protein antibody
30 kDa adipocyte complement-related protein antibody
Adipocyte C1q and collagen domain containing protein antibody
Adipocyte complement related 30 kDa protein antibody
Adipocyte complement related protein of 30 kDa antibody
Adipocyte complement-related 30 kDa protein antibody
adipocyte-specific secretory protein antibody
Adiponectin precursor antibody
adiponectin, C1Q and collagen domain containing antibody
Adipose most abundant gene transcript 1 antibody
Adipose most abundant gene transcript 1 protein antibody
Adipose specific collagen like factor antibody
APM 1 antibody
C1q and collagen domain-containing protein antibody
Gelatin binding protein antibody
Gelatin binding protein 28 antibody
Gelatin-binding protein antibody
References for Anti-Adiponectin antibody (ab18839)
This product has been referenced in:
Chabrolle C et al. Adiponectin increases insulin-like growth factor I-induced progesterone and estradiol secretion in human granulosa cells. Fertil Steril92:1988-96 (2009).
Read more (PubMed: 19081562) »
Chabrolle C et al. Regulation of adiponectin and its receptors in rat ovary by human chorionic gonadotrophin treatment and potential involvement of adiponectin in granulosa cell steroidogenesis. Reproduction133:719-31 (2007).
Read more (PubMed: 17504916) »