Canine Adiponectin ELISA

Canine Adiponectin ELISA

96-well strip plate

Adiponectin is identified as a 30 kDa adipokine that is secreted from the adipose tissue into circulating blood and influences systemic metabolism. Its expression is inversely correlated to insulin resistance. Adiponectin is also known by the following names: Acrp30, AdipoQ, APM-1 and GBP28. It circulates in μg/mL quantities and has a structural homology with type VIII collagen, hibernation protein, and C1q. In contrast to the majority of secreted proteins from adipose tissue which are elevated in obesity, adiponectin appears to be either decreased or unaltered with degree of adiposity. More intriguingly, adiponectin seems to ameliorate the obesity related risk factors unlike other adipose tissue secretory proteins which contribute toward the health risks associated with obesity, diabetes, and cardiovascular risks. Adiponectin also has an insulin sensitizing effect, making it an excellent candidate in drug development for obesity and diabetes. Circulating adiponectin levels seem to be an excellent biochemical marker for improved insulin resistance in obese and diabetic states.

ELISA

Room Temperature, 4 hour assay using 50 µL sample size (serum/plasma: 1:2000 dilution)

Canine

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This gene is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes.

FUNCTION: SwissProt: Q15848 # Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.
SIZE: 244 amino acids; 26414 Da
SUBUNIT: Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionnally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and secreted into plasma.DOMAIN:SwissProt: Q15848 The C1q domain is commonly called the globular domain.
PTM: Hydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. & HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin- sensitizing activity of adiponectin in hepatocytes (By similarity). & O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. & Not N-glycosylated.
DISEASE: SwissProt: Q15848 # Defects in ADIPOQ are the cause of adiponectin deficiency [MIM:605441]. The result is a very low concentration of plasma adiponectin. Decreased adiponectin plasma levels are associated with obesity insulin resistance, and diabetes type 2.
SIMILARITY: Contains 1 C1q domain. & Contains 1 collagen-like domain.
MISCELLANEOUS: Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form. & HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW- complex secretion (By similarity). In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.

88.2 - 100%

0.048 ng/mL

• Q15848
• Q76C76

• Inter-assay: 0.5 - 9.0%
• Intra-assay: 2.9 – 4.2%

95.4–100.5%

• Fluorescent
• Colorimetric

• ADIPOQ
• ACDC
• ACRP30
• APM1
• GBP28

Canine Adiponectin ELISA

0.137 – 100 ng/mL adiponection

Human Adiponectin - 33%
Rat Adiponectin - 100%
Mouse Adiponectin - Not Detectable
Cytokines (Mouse, Rat, Human) - Not Detectable

Adiponectin