CircuLex Dog Adiponectin ELISA Kit

  • Applications
    • ELISA
  • Code # CY-8052
  • Size 96 Assays
  • Price
    $497.49
Specifications

Background

Adiponectin, also referred 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 (1, 2). Adiponectin forms homotrimers, which are the building blocks for higher order complexes found circulating in serum (3, 4). Circulating Adiponectin levels are high (5-30 g/mL), accounting for approximately 0.01% of total plasma protein (5-8). Adiponectin receptors AdipoR1 and AdipoR2 have been recently cloned; AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver (9). Paradoxically, adipose tissue-expressed adiponectin levels are inversely related to the degree of adiposity (10,11). A reduction in adiponectin serum levels is accompanied by insulin resistance states, such as obesity and type 2 diabetes mellitus (12, 13). It is also reported in patients with coronary artery disease (13). 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 high-density 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 (14). Injection of Adiponectin into non-obese diabetic mice leads to an insulin-independent decrease in glucose levels (15). This is likely due to insulin-sensitizing effects involving Adiponectin-regulation of triglyceride metabolism (15). A truncated form of Adiponectin (gAdiponectin) containing only the C-terminal globular domain has been identified in the blood, and recombinant gAdiponectin has been shown to regulate weight reduction as well as free fatty acid oxidation in mouse muscle and liver (16, 17). The full-length recombinant Adiponectin protein is apparently less potent at mediating these effects (16, 17).
  • Application:
    ELISA
  • Components:
    • Microplate
    • 10X Wash Buffer
    • Dilution Buffer
    • Dog Adiponectin Standard
    • HRP conjugated Detection Antibody
    • Substrate Reagent, Stop Solution
  • Description:

    The CycLex Research Product CircuLex Dog Adiponectin ELISA Kit is used for the quantitative measurement of dog adiponectin in serum, plasma, tissue culture medium and other biological media. It can be used for 96 Assays.

  • Product Type:
    ELISA Kit
  • Research Area:
    Metabolism
  • Short Description:

    CircuLex Dog Adiponectin ELISA Kit.

  • Size:
    96 Assays
Citations
  1. Li G et al. Comparison of plasma lipoprotein profiles and malondialdehyde between hyperlipidemia dogs with/without treatment. BMC Vet Res. 10, 67 (2014),
  2. Li GB, Lee P, Mori N, Yamamoto I, Kawasumi K, Tanabe H, Arai T; Supplementing five-point body condition score with body fat percentage increases the sensitivity for assessing overweight status of small to medium sized dogs. Veterinary Medicine: Research and Reports 3, 71, 2012,
  3. Mori N, Sakai M, Yamamoto I and Arai T; Alternation of Physical Indexes and Plasma Biochemical Makers in Overweight Dogs Induced by High-Fat Diet Feeding. Res J Vet Sci 4, 14-19, 2011
References
  1. Maeda, K. et al. (1996) Biochem. Biophys. Res. Commun. 221:286.
  2. Kishore, U. and K.B. Reid (2000) Immunopharmacology 49:159.
  3. Shapiro, L. and P.E. Scherer (1998) Curr. Biol. 8:335.
  4. Nakano, Y. et al. (1996) J. Biochem. (Tokyo) 120:803.
  5. Scherer, P.E. et al. (1995) J. Biol. Chem. 270:26746.
  6. Fruebis, J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:2005.
  7. Berg, A.H. et al. (2002) Trends Endocrinol. Metab. 13:84.
  8. Arita, Y. et al. (1999) Biochem. Biophys. Res. Commun. 257:79.
  9. Yamauchi, T. et al. (2003) Nature 423:762.
  10. Stefan, N. et al. (2002) J. Clin. Endocrinol. Metab. 87:4652.
  11. Matsubara, M. et al. (2002) Eur. J. Endocrinol. 147:173.
  12. Weyer, C. et al. (2001) J. Clin. Endocrinol. Metab. 86:1930.
  13. Hotta, K. et al. (2000) Arterioscler. Thromb. Vasc. Biol. 20:1595.
  14. Tomas, E. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16309.
  15. Berg, A.H. et al. (2001) Nat. Med. 7:947.
  16. Fruebis, J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:2005.
  17. Yamauchi, T. et al. (2001) Nat. Med. 7:941.