Key features and details
- Sensitivity: 0.62 ng/ml
- Range: 0.391 ng/ml - 25 ng/ml
- Sample type: Cell culture supernatant, Plasma, Serum, Tissue Lysate, Urine
- Detection method: Colorimetric
- Assay type: Sandwich (quantitative)
- Reacts with: Mouse
Product nameMouse Adiponectin ELISA Kit
See all Adiponectin kits
Intra-assay Sample n Mean SD CV% Overall 6.2% Inter-assay Sample n Mean SD CV% Overall 10.4%
Sample typeCell culture supernatant, Urine, Serum, Plasma, Tissue Lysate
Assay typeSandwich (quantitative)
Sensitivity= 0.62 ng/ml
Range0.391 ng/ml - 25 ng/ml
Assay time4h 00m
Assay durationMultiple steps standard assay
Species reactivityReacts with: Mouse
Adiponectin Mouse in vitro ELISA (enzyme-linked immunosorbent assay) kit is designed for the quantitative measurement of Adiponectin levels in urine, plasma, serum and cell culture supernatants.
An Adiponectin specific antibody has been precoated onto 96-well plates and blocked. Standards or test samples are added to the wells and subsequently an Adiponectin specific biotinylated detection antibody is added and then followed by washing with wash buffer. Streptavidin-Peroxidase Conjugate is added and unbound conjugates are washed away with wash buffer. TMB is then used to visualize Streptavidin-Peroxidase enzymatic reaction. TMB is catalyzed by Streptavidin-Peroxidase to produce a blue color product that changes into yellow after adding acidic stop solution. The density of yellow coloration is directly proportional to the amount of Adiponectin captured in plate.
The entire kit may be stored at -20°C for long term storage before reconstitution - Avoid repeated freeze-thaw cycles.
Storage instructionsStore at -20°C. Please refer to protocols.
Components 1 x 96 tests 100X Streptavidin-Peroxidase Conjugate 1 x 80µl 10X Diluent N Concentrate 1 x 30ml 20X Wash Buffer Concentrate 2 x 30ml 70X Biotinylated Mouse Adiponectin Antibody 1 x 90µl Adiponectin Microplate (12 x 8 well strips) 1 unit Adiponectin Standard 1 vial Chromogen Substrate 1 x 7ml Sealing Tapes 3 units Stop Solution 1 x 11ml
- Pathways and Processes
- Metabolic signaling pathways
- Lipid and lipoprotein metabolism
- Fatty acids
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.
Sequence similaritiesContains 1 C1q domain.
Contains 1 collagen-like domain.
DomainThe C1q domain is commonly called the globular domain.
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.
- Information by UniProt
- 30 kDa adipocyte complement related protein
- 30 kDa adipocyte complement-related protein
ab108785 has been referenced in 17 publications.
- Miranda MA et al. Dietary iron interacts with genetic background to influence glucose homeostasis. Nutr Metab (Lond) 16:13 (2019). PubMed: 30820238
- Zhang JK et al. ß3-Adrenergic Activation Improves Maternal and Offspring Perinatal Outcomes in Diet-Induced Prepregnancy Obesity in Mice. Obesity (Silver Spring) 27:1482-1493 (2019). PubMed: 31328894
- Schaar A et al. Ca2+ entry via TRPC1 is essential for cellular differentiation and modulates secretion via the SNARE complex. J Cell Sci 132:N/A (2019). PubMed: 31182642
- Ishay-Ronen D et al. Gain Fat-Lose Metastasis: Converting Invasive Breast Cancer Cells into Adipocytes Inhibits Cancer Metastasis. Cancer Cell 35:17-32.e6 (2019). PubMed: 30645973
- Beaumatin F et al. mTORC1 Activation Requires DRAM-1 by Facilitating Lysosomal Amino Acid Efflux. Mol Cell 76:163-176.e8 (2019). PubMed: 31492633