Mouse Adiponectin ELISA Kit (ab108785)
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
Overview
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Product name
Mouse Adiponectin ELISA Kit
See all Adiponectin kits -
Detection method
Colorimetric -
Precision
Intra-assay Sample n Mean SD CV% Overall 6.2% Inter-assay Sample n Mean SD CV% Overall 10.4% -
Sample type
Cell culture supernatant, Urine, Serum, Plasma, Tissue Lysate -
Assay type
Sandwich (quantitative) -
Sensitivity
= 0.62 ng/ml -
Range
0.391 ng/ml - 25 ng/ml -
Recovery
100 %
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Assay time
4h 00m -
Assay duration
Multiple steps standard assay -
Species reactivity
Reacts with: Mouse -
Product overview
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.
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Platform
Microplate
Properties
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Storage instructions
Store 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 -
Research areas
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Function
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. -
Tissue specificity
Synthesized exclusively by adipocytes and secreted into plasma. -
Involvement in disease
Defects 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 similarities
Contains 1 C1q domain.
Contains 1 collagen-like domain. -
Domain
The 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. -
Cellular localization
Secreted. - Information by UniProt
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Alternative names
- 30 kDa adipocyte complement related protein
- 30 kDa adipocyte complement-related protein
- ACDC
see all -
Database links
- Entrez Gene: 11450 Mouse
- SwissProt: Q60994 Mouse
- Unigene: 3969 Mouse
Images
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Sandwich ELISA - Adiponectin Mouse ELISA kit (ab108785)Adiponectin measured in biological fluids with background signal subtracted (duplicates +/- SD).
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Typical Standard CurveRepresentative Standard Curve using ab108785
Datasheets and documents
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SDS download
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Datasheet download
References (26)
ab108785 has been referenced in 26 publications.
- Kakehashi A et al. Cache Domain Containing 1 Is a Novel Marker of Non-Alcoholic Steatohepatitis-Associated Hepatocarcinogenesis. Cancers (Basel) 13:N/A (2021). PubMed: 33802238
- Tang Y et al. Rapid responses of adipocytes to iron overload increase serum TG level by decreasing adiponectin. J Cell Physiol N/A:N/A (2021). PubMed: 33855731
- Feng B et al. Silymarin ameliorates the disordered glucose metabolism of mice with diet-induced obesity by activating the hepatic SIRT1 pathway. Cell Signal 84:110023 (2021). PubMed: 33901577
- Gutiérrez G et al. Serjanic Acid Improves Immunometabolic Markers in a Diet-Induced Obesity Mouse Model. Molecules 25:N/A (2020). PubMed: 32218297
- Kim DY et al. Angiotensin AT1 receptor antagonism by losartan stimulates adipocyte browning via induction of apelin. J Biol Chem 295:14878-14892 (2020). PubMed: 32839272