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Adiponectin ELISA Kit (Adiponectin, High Molecular Weight)

Details for Product ADIPOQ ELISA Kit No. ABIN249421, Supplier: Log in to see
  • ACDC
  • ACRP30
  • ADPN
  • APM-1
  • APM1
  • GBP28
  • 30kDa
  • APN
  • Acdc
  • Acrp30
  • adipo
  • apM1
  • ADN
Mouse (Murine) Adiponectin ELISA Kit
Mouse (Murine), Rat (Rattus)
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Specificity Using two antibodies this kit can assay mouse/rat high molecular weight adiponectin (HMW). Precision and reproducibility: (1) Within assay variation (2 samples, 5 replicates assay) Average C.V. is less than 5%. (2) Reproducibility (3 samples, duplicates assays, 4 days) Average C.V. is less than 5%.
Alternative Name Adiponectin HMW (ADIPOQ ELISA Kit Abstract)
Background Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 aminoacid protein, the product of the apM1 gene, which is sphysiologically active and specifically and highly expressed in adipose cells. The protein belongs to the soluble defence collagen superfamily, it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. Adiponectin forms homotrimers, which are the building blocks for higher order complexes found circulating in serum. Together, these complexes make up approximately 0.01% of total serum protein. Adiponectin receptors AdipoR1 and AdipoR2 have been recently cloned, AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. Paradoxically, adipose tissue-expressed adiponectin levels are inversely related to the degree of adiposity. Adiponectin concentrations correlate negatively with glucose, insulin, triglyceride concentrations, liver fat content and body mass index and positively with high-density lipoprotein-cholesterol levels, hepatic insulin sensitivity and insulin-stimulated glucose disposal. Adiponectin has been shown to increase insulin sensitivity and decrease plasma glucose by increasing tissue fat oxidation. Of particular interest is that low adiponectin serum levels predict type 2 diabetes independent of other risk factors. Adiponectin also inhibits the inflammatory processes of atherosclerosis suppressing the expression of adhesion and cytokine molecules in vascular endothelial cells and macrophages, respectively. This adipokine plays a role as a scaffold of newly formed collagen in myocardial remodelling after ischaemic injury and also stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signalling in endothelial cells. Low serum adiponectin levels are found in patients with coronary artery disease. Moreover, high circulating levels of adiponectin are associated with decreased risk of myocardial infarction, independent of other factors. Altogether, adiponectin has the potential to become a clinically relevant parameter to be measured routinely in subjects at risk for type 2 diabetes, atherosclerosis and the metabolic syndrome.
Research Area Metabolism
Pathways AMPK Signaling
Application Notes Sample requirements: 50
Restrictions For Research Use only
Buffer (A) Anti-adiponectin-coated plate - 96 wells(8x12) / 1 plate (B) Standard adiponectin solution (2000ng/ml) - 200 ul / 1 vial (C) Buffer solution - 60ml/ 1 bottle (D) HRP-conjugated anti-adiponectin - 100 ul / 1 vial (F) Chromogenic substrate reagent (TMB)
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Background publications Schraw, Wang, Halberg et al.: "Plasma adiponectin complexes have distinct biochemical characteristics." in: Endocrinology, Vol. 149, Issue 5, pp. 2270-82, 2008 (PubMed).

Westphal, Luley: "Preferential increase in high-molecular weight adiponectin after niacin." in: Atherosclerosis, Vol. 198, Issue 1, pp. 179-83, 2008 (PubMed).

Nishimura, Morimoto, Matsudaira et al.: "Ratio of high-, medium-, and low-molecular weight serum adiponectin to the total adiponectin value in children." in: The Journal of pediatrics, Vol. 151, Issue 5, pp. 545-7, 547.e1-2, 2007 (PubMed).

Sinha, Songer, Xiao et al.: "Analytical validation and biological evaluation of a high molecular-weight adiponectin ELISA." in: Clinical chemistry, Vol. 53, Issue 12, pp. 2144-51, 2008 (PubMed).

Seino, Hirose, Saito et al.: "High molecular weight multimer form of adiponectin as a useful marker to evaluate insulin resistance and metabolic syndrome in Japanese men." in: Metabolism: clinical and experimental, Vol. 56, Issue 11, pp. 1493-9, 2007 (PubMed).

Liu, Retnakaran, Hanley et al.: "Total and high molecular weight but not trimeric or hexameric forms of adiponectin correlate with markers of the metabolic syndrome and liver injury in Thai subjects." in: The Journal of clinical endocrinology and metabolism, Vol. 92, Issue 11, pp. 4313-8, 2007 (PubMed).

Schober, Neumeier, Weigert et al.: "Low molecular weight adiponectin negatively correlates with the waist circumference and monocytic IL-6 release." in: Biochemical and biophysical research communications, Vol. 361, Issue 4, pp. 968-73, 2007 (PubMed).

Petersen, Dufour, Savage et al.: "The role of skeletal muscle insulin resistance in the pathogenesis of the metabolic syndrome." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Issue 31, pp. 12587-94, 2007 (PubMed).

Torigoe, Matsui, Ogawa et al.: "Impact of the high-molecular-weight form of adiponectin on endothelial function in healthy young men." in: Clinical endocrinology, Vol. 67, Issue 2, pp. 276-81, 2007 (PubMed).

Semple, Halberg, Burling et al.: "Paradoxical elevation of high-molecular weight adiponectin in acquired extreme insulin resistance due to insulin receptor antibodies." in: Diabetes, Vol. 56, Issue 6, pp. 1712-7, 2007 (PubMed).

Suzuki, Wilson-Kubalek, Wert et al.: "The oligomeric structure of high molecular weight adiponectin." in: FEBS letters, Vol. 581, Issue 5, pp. 809-14, 2007 (PubMed).

Salani, Briatore, Andraghetti et al.: "High-molecular weight adiponectin isoforms increase after biliopancreatic diversion in obese subjects." in: Obesity (Silver Spring, Md.), Vol. 14, Issue 9, pp. 1511-4, 2006 (PubMed).

Takemura, Osuga, Koga et al.: "Selective increase in high molecular weight adiponectin concentration in serum of women with preeclampsia." in: Journal of reproductive immunology, Vol. 73, Issue 1, pp. 60-5, 2007 (PubMed).

Wang, Lam, Chan et al.: "Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex." in: The Journal of biological chemistry, Vol. 281, Issue 24, pp. 16391-400, 2006 (PubMed).

Richards, Stephens, Charlton et al.: "Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications." in: Molecular endocrinology (Baltimore, Md.), Vol. 20, Issue 7, pp. 1673-87, 2006 (PubMed).

Xu, Chan, Hoo et al.: "Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes." in: The Journal of biological chemistry, Vol. 280, Issue 18, pp. 18073-80, 2005 (PubMed).

Wang, Lam, Xu et al.: "Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner." in: The Journal of biological chemistry, Vol. 280, Issue 18, pp. 18341-7, 2005 (PubMed).

Waki, Yamauchi, Kamon et al.: "Generation of globular fragment of adiponectin by leukocyte elastase secreted by monocytic cell line THP-1." in: Endocrinology, Vol. 146, Issue 2, pp. 790-6, 2005 (PubMed).

Tonelli, Li, Kishore et al.: "Mechanisms of early insulin-sensitizing effects of thiazolidinediones in type 2 diabetes." in: Diabetes, Vol. 53, Issue 6, pp. 1621-9, 2004 (PubMed).

Pajvani, Hawkins, Combs et al.: "Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity." in: The Journal of biological chemistry, Vol. 279, Issue 13, pp. 12152-62, 2004 (PubMed).

Waki, Yamauchi, Kamon et al.: "Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin." in: The Journal of biological chemistry, Vol. 278, Issue 41, pp. 40352-63, 2003 (PubMed).