Offline mode
Innovation in alcohol marker testing.
PEthLC-MS
PEth offers an ethanol detection
window of up to 4 weeks.read more

Intended use

The Adiponectin ELISA is intended to be used for quantitative measurement of human Adiponectin in human serum and plasma samples.

Introduction

Adiponectin is a 30kDa protein which percentage in serum proteins is 0.01%. It is mainly synthesized by adipocytes, but also muscle cells and hepatocytes have the ability to synthesize Adiponectin. It consists of a Collagen-like N-terminal and a globular C-terminal domain [1]. In vivo Adiponectin appears with different oligomers. Beside the trimer and ditrimer also high molecular multimers exist [1-3]. Two different receptors are known, both receptors are ubiquitary expressed, though the distribution in the tissues varies. The Adiponectin Receptor 1 (AdipoR1) is especially in muscle- and AdipoR2 in liver tissue synthesized [4].

Several studies show, that adiponectin correlates negatively with BMI and thus it could have relevance for the energy metabolism for example through the regulation of fatty acid oxidation. Beside the correlation with BMI, Adiponectin level is associated with the Insulin-Resistance [5-7] and so also linked with Type II Diabetes. Adiponectin is associated also with glucose- und lipometabolism [8, 9]. The formerly proposed diagnostic value of the high molecular weight form of adiponectin was not verified using a commercially available test system for the determination of HMW adiponectin [10].

Blueher et al. evaluated the Adiponektin ELISA regarding its diagnostic value in diagnosis of insulin resistance. Results of ROC analysis showed an area under curve of 0.92, which indicates a diagnostic value [10]. Furthermore adiponectin is involved in inflammatory processes [11-15] and therewith it is of importance for appearance of arteriosclerosis [4, 5, 16] and coronaritis [17, 18], thus the determination of Adiponectin level in plasma could serve to estimate the risk of coronary disease [19, 20]. Beside this Adiponectin influences further physiological processes as for example the angiogenesis [21, 22].

For concrete data please consult the Instruction for Use in the download box on the top right side.

  1. Nakano, Y., et al., Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J Biochem (Tokyo), 1996. 120(4): p. 803-12.
  2. Pajvani, U.B., et al., Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin. Implications fpr metabolic regulation and bioactivity. J Biol Chem, 2003. 278(11): p. 9073-85.
  3. Tsao, T.S., et al., Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways. J Biol Chem, 2003. 278(50): p. 50810-7.
  4. Shimada, K., T. Miyazaki, and H. Daida, Adiponectin and atherosclerotic disease. Clin Chim Acta, 2004. 344(1-2): p. 1-12.
  5. Higashiura, K., et al., Correlations of adiponectin level with insulin resistance and atherosclerosis in Japanese male populations. Clin Endocrinol (Oxf), 2004. 61(6): p. 753-9.
  6. Spranger, J., et al., Adiponectin is independently associated with insulin sensitivity in women with polycystic ovary syndrome. Clin Endocrinol (Oxf), 2004. 61(6): p. 738-46.
  7. Zoico, E., et al., Adipocytokines, fat distribution, and insulin resistance in elderly men and women. J Gerontol A Biol Sci Med Sci, 2004. 59(9): p. M935-9.
  8. Ye, J.M., et al., PPARalpha /gamma ragaglitazar eliminates fatty liver and enhances insulin action in fat-fed rats in the absence of hepatomegaly. Am J Physiol Endocrinol Metab, 2003. 284(3): p. E531-40.
  9. Yamauchi, T., et al., Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat Med, 2002. 8(11): p. 1288-95.
  10. Blüher (Blueher), M., et al., Total and high-molecular weight adiponectin in relation to metabolic variables at baseline and in response to an exercise treatment program: comparative evaluation of three assays. Diabetes Care, 2007. 30(2): p. 280-5.
  11. Delaigle, A.M., et al., Induction of adiponectin in skeletal muscle by inflammatory cytokines: in vivo and in vitro studies. Endocrinology, 2004. 145(12): p. 5589-97.
  12. Winzer, C., et al., Plasma adiponectin, insulin sensitivity, and subclinical inflammation in women with prior gestational diabetes mellitus. Diabetes Care, 2004. 27(7): p. 1721-7.
  13. Xydakis, A.M., et al., Adiponectin, inflammation, and the expression of the metabolic syndrome in obese individuals: the impact of rapid weight loss through caloric restriction. J Clin Endocrinol Metab, 2004. 89(6): p. 2697-703.
  14. Motoshima, H., et al., Adiponectin suppresses proliferation and superoxide generation and enhances eNOS activity in endothelial cells treated with oxidized LDL. Biochem Biophys Res Commun, 2004. 315(2): p. 264-71.
  15. Wolf, A.M., et al., Adiponectin induces the anti-inflammatory cytokines IL-10 and IL-1RA in human leukocytes. Biochem Biophys Res Commun, 2004. 323(2): p. 630-5.
  16. Okamoto, Y., et al., Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice. Circulation, 2002. 106(22): p. 2767-70.
  17. Schlegel, A., Adiponectin and risk of coronary heart disease. Jama, 2004. 292(1): p. 40; author reply 40.
  18. Choi, K.M., et al., Inflammation, Insulin Resistance, and Glucose Intolerance in Acute Myocardial Infarction Patients without a Previous Diagnosis of Diabetes Mellitus. J Clin Endocrinol Metab, 2004.
  19. Nakamura, Y., et al., Implications of plasma concentrations of adiponectin in patients with coronary artery disease. Heart, 2004. 90(5): p. 528-33.
  20. Pischon, T., et al., Plasma adiponectin levels and risk of myocardial infarction in men. Jama, 2004. 291(14): p. 1730-7.
  21. Shibata, R., et al., Adiponectin stimulates angiogenesis in response to tissue ischemia through stimulation of amp-activated protein kinase signaling. J Biol Chem, 2004. 279(27): p. 28670-4.
  22. Fernandez-Real, J.M., et al., Adiponectin is associated with vascular function independent of insulin sensitivity. Diabetes Care, 2004. 27(3): p. 739-45.

Our Product Families

Our comprehensive immunoassay portfolio includes a number of specialty diagnostic immunoassays for endocrinology, immunology and autoimmunity, as well as for diagnosis of multiple infectious diseases. We are pioneers and market leaders in saliva diagnostics, with over 40 years of experience supplying a broad portfolio of luminescence- and ELISA-based tests, including our highly acclaimed HMGB1 and MuSK-Ab ELISAs.

And as experts in laboratory automation, we can support our customers with the protocols for open ELISA platforms, such as the Freedom EVOlyzer or Thunderbolt®.

All products are only available for sale to laboratory professionals and may not be available in all countries. Availability and regulatory status may vary across regions depending on local country-specific registration. Please always read and follow the instructions for use. 

Image
Autoimmunity
Image
Complementary Medicine
Image
Endocrinology
Image
Infectious Diseases
Image
Immunology
Image
Neurodegeneration & Neurotransmitters

All of our assays have been designed and manufactured to meet the highest global regulatory requirements and quality standards. Tecan is certified under ISO 9001:2015, ISO 13485:2016 and is audited by a notified body according to Medical Device Single Audit Program (MDSAP).

Image on background

This is who we are.

As part of the Tecan Group, we have a leading market position in diagnostics and research, with over 40 years of experience in the development, manufacture and supply of enzyme-, radiolabel- and luminescence-based immunoassays.

Our range of high-quality immunoassays is supported by a diverse portfolio of automated solutions, making us the perfect partner for you and your customers.

Learn more >
Happy to help.
Customer Service
Product Support

At Tecan, we are driven to improve people’s lives and health.

Follow tecan