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Adiponectin Mouse ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30 kDa protein, ACRP30, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein, ADIPOQ, ACDC, APM1, GBP28
  • Species:Mouse
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Cat. No. Size Price


RD293023100R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum

Sample Requirements

10 µl/well

Storage/Expiration

Store the kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

0.25–8 ng/ml

Limit of Detection

0.079 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 2.5%

Inter-assay (Run-to-Run)

n = 5; CV = 4.3%

Spiking Recovery

97,40%

Dilutation Linearity

88,20%

Crossreactivity

  • bovine Non-detectable
  • cat Non-detectable
  • dog Non-detectable
  • goat Non-detectable
  • hamster Non-detectable
  • horse Non-detectable
  • human Non-detectable
  • monkey Non-detectable
  • pig Non-detectable
  • rabbit Non-detectable
  • rat Non-detectable
  • sheep Non-detectable
  • chicken Not tested
  • mouse Yes
Summary

Features

  • The total assay time is less than 3 hours.
  • The kit measures mouse serum Adiponectin/Acrp30.
  • Quality Controls are mouse serum based.
  • Components of the kit are provided ready-to-use, concentrated and lyophilized.

Research topic

Animal studies, Chronic renal failure, Coronary artery disease, Diabetology - Other Relevant Products, Energy metabolism and body weight regulation

Summary

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 physiologically active and
specifically and highly expressed in adipose cells (adipokine). 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. 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. A reduction in adiponectin serum levels is accompanied by insulin resistance
states, such as obesity and type 2 diabetes mellitus. It is also reported in patients with coronary
artery disease. Increased adiponectin levels are associated with type 1 diabetes mellitus,
anorexia nervosa and chronic renal failure. Adiponectin concentrations correlate negatively
with glucose, insulin, triglyceride concentrations and body mass index and positively with highdensity
lipoprotein-cholesterol levels and insulin-stimulated glucose disposal.
Adiponectin has been shown to increase insulin sensitivity and decrease plasma glucose by
increasing tissue fat oxidation. It 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.

References to Product

References

  • Adams AC, Yang C, Coskun T, Cheng CC, Gimeno RE, Luo Y, Kharitonenkov A. The breadth of FGF21's metabolic actions are governed by FGFR1 in adipose tissue. Mol Metab. 2012;2 (1):31-7
  • Berner HS, Lyngstadaas SP, Spahr A, Monjo M, Thommesen L, Drevon CA, Syversen U, Reseland JE. Adiponectin and its receptors are expressed in bone-forming cells. Bone . Oct;35(4):842-9 (2004)
  • Giri S, Rattan R, Hag E, Khan M, Yasmin R, Won JS, Key L, Singh AK, Singh I. AICAR inhibits adipocyte differentiation in 3T3L1 and restores metabolic alterations in diet-induced obesity mice model. Nutr Metab (Lond) . Aug 10;3:31 (2006)
  • Hennige AM, Staiger H, Wicke C, Machicao F, Fritsche A, Haring HU, Stefan N. Fetuin-A induces cytokine expression and suppresses adiponectin production. PLoS ONE. 2008;3 (3):e1765
  • Lang P, van Harmelen V, Ryden M, Kaaman M, Parini P, Carneheim C, Cassady AI, Hume DA, Andersson G, Arner P. Monomeric tartrate resistant acid phosphatase induces insulin sensitive obesity. PLoS One. 2008;3 (3):e1713
  • Sainz N, Rodriguez A, Catalan V, Becerril S, Ramirez B, Gomez-Ambrosi J, Fruhbeck G. Leptin administration downregulates the increased expression levels of genes related to oxidative stress and inflammation in the skeletal muscle of ob/ob mice. Mediators Inflamm. 2010;2010:784343
  • Shimizu T, Yamakuchi M, Biswas KK, Aryal B, Yamada S, Hashiguchi T, Maruyama I. HMGB1 is secreted by 3T3-L1 adipocytes through JNK signaling and the secretion is partially inhibited by adiponectin. Obesity (Silver Spring). 2016 Jul 19;
References to Summary

References to Adiponectin

  • Lam KS, Xu A. Adiponectin: protection of the endothelium. Curr Diab Rep. 2005, 5, 254–259.
  • Ding X, Saxena NK, Lin S, Xu A, Srinivasan S, Anania FA. The roles of leptin and adiponectin: a novel paradigm in adipocytokine regulation of liver fibrosis and stellate cell biology. Am J Pathol. 2005, 166, 1655–1669.
  • Xu A, Chan KW, Hoo RL, Wang Y, Tan KC, Zhang J, Chen B, Lam MC, Tse C, Cooper GJ, Lam KS. Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes. J Biol Chem. 2005, 280, 18073–18080.
  • Wang Y, Lam KS, Xu JY, Lu G, Xu LY, Cooper GJ, Xu A. Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner. J Biol Chem. 2005, 280, 18341–18347.
  • Ouchi N, Kobayashi H, Kihara S, Kumada M, Sato K, Inoue T, Funahashi T, Walsh K. Adiponectin stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signaling in endothelial cells. J Biol Chem. 2004, 279, 1304–1309.
  • Ishikawa Y, Akasaka Y, Ishii T, Yoda-Murakami M, Choi-Miura NH, Tomita M, Ito K, Zhang L, Akishima Y, Ishihara M, Muramatsu M, Taniyama M. Changes in the distribution pattern of gelatinbinding protein of 28 kDa (adiponectin) in myocardial remodelling after ischaemic injury. Histopathology. 2003, 42, 43–52.
  • Diez JJ, Iglesias P. The role of the novel adipocyte-derived hormone adiponectin in human disease. Eur J Endocrinol. 2003, 148, 293–300.
  • Waki H, Yamauchi T, Kamon J, Ito Y, Uchida S, Kita S, Hara K, Hada Y, Vasseur F, Froguel P, Kimura S, Nagai R, Kadowaki T. Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin. J Biol Chem. 2003, 278, 40352–40363.
  • Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature. 2003, 423, 762–769.
  • Yamauchi T, Kamon J, Waki H, Imai Y, Shimozawa N, Hioki K, Uchida S, Ito Y, Takakuwa K, Matsui J, Takata M, Eto K, Terauchi Y, Komeda K, Tsunoda M, Murakami K, Ohnishi Y, Naitoh T, Yamamura K, Ueyama Y, Froguel P, Kimura S, Nagai R, Kadowaki T. Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis. J Biol Chem. 2003, 278, 2461–2468.
  • Daimon M, Oizumi T, Saitoh T, Kameda W, Hirata A, Yamaguchi H, Ohnuma H, Igarashi M, Tominaga M, Kato T. Decreased serum levels of adiponectin are a risk factor for the progression to type 2 diabetes in the Japanese Population: the Funagata study. Diabetes Care. 2003 Jul;26(7):2015–20.
  • Pajvani UB, Du X, Combs TP, Berg AH, Rajala MW, Schulthess T, Engel J, Brownlee M, Scherer PE. Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin. Implications for metabolic regulation and bioactivity. J Biol Chem. 2003, 278, 9073–9085.
  • Spranger J, Kroke A, Mohlig M, Bergmann MM, Ristow M, Boeing H, Pfeiffer AF. Adiponectin and protection against type 2 diabetes mellitus. Lancet. 2003, 361, 226–228.
  • Kondo H, Shimomura I, Matsukawa Y, Kumada M, Takahashi M, Matsuda M, Ouchi N, Kihara S, Kawamoto T, Sumitsuji S, Funahashi T, Matsuzawa Y. Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome. Diabetes. 2002, 51, 2325–2328.
  • Wang Y, Xu A, Knight C, Xu LY, Cooper GJ. Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity. J Biol Chem. 2002, 277, 19521–19529.
  • Tsao TS, Lodish HF, Fruebis J. ACRP30, a new hormone controlling fat and glucose metabolism. Eur J Pharmacol. 2002, 440, 213–21.
  • Das K, Lin Y, Widen E, Zhang
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