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Human Adiponectin ELISA, High Sensitivity (GWB-3CD9AC)



1x96 well plate
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Product Name Human Adiponectin ELISA.
# of Samples 1X96 Assays.
Intended Use The Human Adiponectin ELISA (40-055-200002), High Sensitivity is a sandwich Enzymelinked immunosorbent Assay for the quantitative measurement of human adiponectin in serum, plasma, breast milk, urine, cerebrospinal fluid (CSF) and tissue culture media.
Principle of the test In the GenWay's Human Adiponectin ELISA, standards, quality control and samples are incubated in microtitration wells coated with an antiadiponectin polyclonal antibody. After a thorough wash, polyclonal antiadiponectin antibody labelled with horseradish peroxidase (HRP) is added to the wells and incubated with the immobilized antibody-adiponectin complex. Following another washing step, the remaining HRP-conjugated antibody is allowed to react with the hydrogen peroxide/TMB substrate solution. The reaction is stopped by addition of acidic solution and absorbance of the resulting yellow colour product is measured spectrophotometrically at 450 nm. The absorbance is proportional to the concentration of adiponectin. A standard curve is constructed by plotting absorbance values versus adiponectin concentrations of standards, and concentrations of unknown samples are determined using this standard curve.
Sensitivity and Specificity The assay recognizes natural and recombinant (full length, mutation-modified trimeronly- forming, and globular domain) human Adiponectin. No cross-reactivity has been observed for human Leptin, Leptin Receptor and Resistin at 100 ng/ml.
Among animal species, specific signal was observed (it exhibited dilution linearity) in Rhesus monkey and Cynomolgus monkey sera. The signal was equivalent to 15-19 ?g/ml of human adiponectin.
No signal has been obtained when sera of the following species were measured in the assay: sheep, goat, horse, cow, pig, rabbit.
Dog serum gave a nonspecific medium level signal, rodent sera (hamster, mouse, and rat) gave only very week probably nonspecific signal.
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.
Subunit Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionnally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2.
Subcellular Location Secreted.
Tissue Specificity Synthesized exclusively by adipocytes and secreted into plasma.
Domain The C1q domain is commonly called the globular domain.
  • Hydroxylated 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 (By similarity).
  • O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
  • Not N-glycosylated.
Disease Defects in ADIPOQ are the cause of adiponectin deficiency [MIM:605441]. The result is a very low concentration of plasma adiponectin. Decreased adiponectin plasma levels are associated with obesity insulin resistance, and diabetes type 2.
Pharmaceutical Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.
Miscellaneous Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form.

HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion (By similarity). In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.
Similarity Contains 1 C1q domain.

Contains 1 collagen-like domain.

Additional Information

Name Human Adiponectin ELISA, High Sensitivity (GWB-3CD9AC)
Related Product Names Human Adiponectin ELISA Kit ELISA Kit; Adipocyte, C1q and collagen domain-containing protein; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipose most abundant gene transcript 1 protein; apM-1; Gelatin
Swissprot ID Q15848
NCBI Acc Number NP_004788.1
Molecular Weight 26414
Datasheets/Manuals Printable manual for GWB-3CD9AC
Intended Use Research Use Only