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Manufactured by BioVendor

Adiponectin Human PENTASET

  • Regulatory status:RUO
  • Type:ELISA development kit
  • 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:Human
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Cat. No. Size Price


Discount RD120023 1-for 5x 96-well plates
PubMed Product Details
Technical Data

Type

ELISA development kit

Applications

Serum, Cell culture medium, ELISA, Plasma, Others

Sample Requirements

1 µl/well (Serum, Plasma)

Storage/Expiration

  • Shipping at ambient temperature
  • Store the kit at –20°C after the delivery. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

4.69–150 ng/ml

Summary

Features

The BioVendor PENTASET is a development kit containing specific components including pre-optimized antibody matched pair, recombinant protein standard and streptavidin-HRP required for the development of a sandwich ELISA. Basic set is intended to perform assay on 5 plates.

  • The inserted Product Data Sheet must be read before using this product
  • The kit is intended for experienced ELISA users

Research topic

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

Summary

Adiponectin (244 aa) is expressed in adipose cells. It belongs to the soluble defence collagen superfamily containing collagen VIII a X homologous do-main and C1q-like globular domain. Adiponectin forms covalently bound trimers (LMW), 2 trimers form hexamers (MMW) and their multiples (HMW) circulating in blood. The receptors AdipoR1 and AdipoR2 have been identified. Adiponectin increases insulin sensitivity and decreases 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. This adipokine plays a role as a scaffold of newly formed collagen in myocardial remodelling after ischaemic injury. Adiponectin has become a clinically relevant parameter to be measured in subjects at risk for type 2 diabetes, atherosclerosis and the metabolic syndrome.

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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