Human Adiponectin ELISA Kit | ADIPOQ elisa kit

Human Adiponectin ELISA KIT

Cat. Num. AAA9424808

• Gene Names: ADIPOQ; ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• Reactivity: Human
• Synonyms: Adiponectin; Human Adiponectin ELISA KIT; Human Adiponectin; ADIPOQ elisa kit

• Reactivity: Human
• Specificity: Natural and recombinant Human Adiponectin Ligand

• Assay Type: Solid Phase Sandwich ELISA
• Samples: Cell culture supernatant, serum, plasma (EDTA, citrate, heparin)
• Detection Range: 15.625-1000pg/mL
• Sensitivity: 4pg/mL
• Assay Time: 3 hours
• Sample Volume: 20 uL
• Detection Method: Colorimetric
• Preparation and Storage: Store at 4 degree C

Typical Testing Data/Standard Curve (for reference only)

(Representative standard curve for Adiponectin ELISA. Adiponectin was diluted in serial two-fold steps in Sample Diluent.)

Related Product Information for ADIPOQ elisa kit

Adiponectin, alternately named Adipocyte complement-related protein of 30 kDa (Acrp30), adipoQ, adipose most abundant gene transcript 1 (apM1), and gelatin-binding protein of 28 kDa (GBP28), is an adipocyte-specific, secreted protein with potential roles in glucose and lipid homeostasis. Circulating Adiponectin levels are high, accounting for approximately 0.01% of total plasma protein (1-4). Adiponectin contains a modular structure that includes an N-terminal collagen-like domain followed by a C-terminal globular domain with significant sequence and structural resemblance to the complement factor C1q (1, 5, 6). Although they share little sequence identity, similar three-dimensional structure and certain conserved amino acid residues suggest an evolutionary link between the C1q-like domain of Adiponectin and members of the TNF superfamily (7). Adiponectin assembles into different complexes including trimers (low molecular weight), hexamers (middle molecular weight), and higher order oligomeric structures (high molecular weight) that may affect biological activity (1, 7, 8). Adiponectin is induced during adipocyte differentiation and its secretion is stimulated by insulin (1, 9). Two receptors for Adiponectin, termed AdipoR1 and AdipoR2, have been cloned (10). Although functionally distinct from G-protein-coupled receptors, the genes encode predicted proteins containing 7 transmembrane domains. AdipoR1 is highly expressed in skeletal muscle, while AdipoR2 is primarily found in hepatic tissues.Injection of Adiponectin into non-obese diabetic mice leads to an insulin-independent decrease in glucose levels (11). This is likely due to insulin-sensitizing effects involving Adiponectin regulation of triglyceride metabolism (11). 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 (2, 12). The full-length recombinant Adiponectin protein is apparently less potent at mediating these effects (2, 12). The mechanism underlying the role of Adiponectin in lipid oxidation may involve the regulation of expression or activity of proteins associated with triglyceride metabolism including CD36, acyl CoA oxidase, AMPK, and PPARg (12-14).Although Adiponectin-regulation of glucose and lipid metabolism in humans is less clear, similar mechanisms may also be in place (15). A negative correlation between obesity and circulating Adiponectin has been well established (6, 16, 17), and Adiponectin levels increase concomitantly with weight loss (18). Decreased Adiponectin levels are associated with insulin resistance and hyperinsulinemia, and patients with type-2 diabetes are reported to exhibit decreased circulating Adiponectin (19, 20). Thiazolidinediones, a class of insulin-sensitizing, anti-diabetic drugs, elevate Adiponectin in insulin-resistant patients (21). In addition, high Adiponectin levels are associated with a reduced risk of type-2 diabetes (22). Using magnetic resonance spectroscopy it has been demonstrated that intracellular lipid content in human muscle negatively correlates with Adiponectin levels, potentially due to Adiponectin-induced fatty acid oxidation (15).Adiponectin may also play anti-atherogenic and anti-inflammatory roles. Adiponectin plasma levels are decreased in patients with coronary artery disease (20). Furthermore, neointimal thickening of damaged arteries is exacerbated in Adiponectin-deficient mice and is inhibited by exogenous Adiponectin (23). Adiponectin inhibits endothelial cell expression of adhesion molecules in vitro, suppressing the attachment of monocytes (24). In addition, Adiponectin negatively regulates myelomonocytic progenitor cell growth and TNF-a production in macrophages (25, 26).

NCBI and Uniprot Product Information

• NCBI GI #: 295317372
• NCBI GeneID: 9370
• NCBI Accession #: NP_001171271.1
• NCBI GenBank Nucleotide #: NM_001177800.1
• UniProt Accession #: Q15848; Q58EX9
• Molecular Weight: 26,414 Da
• NCBI Official Full Name: adiponectin
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: ADIPOQ
• NCBI Official Synonym Symbols: ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• NCBI Protein Information: adiponectin
• UniProt Protein Name: Adiponectin
• Protein Family: Adiponectin
• UniProt Gene Name: ADIPOQ
• UniProt Synonym Gene Names: ACDC; ACRP30; APM1; GBP28; ACRP30; apM-1

NCBI Description

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. Mutations in this gene are associated with adiponectin deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Apr 2010]

Uniprot Description

adiponectin: 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. 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 aditionally 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. Interacts with CTRP9A via the C1q domain (heterotrimeric complex). Synthesized exclusively by adipocytes and secreted into plasma.

Protein type: Endoplasmic reticulum; Hormone; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 3q27.3

Cellular Component: cell surface; endoplasmic reticulum; extracellular region; extracellular space

Molecular Function: hormone activity; identical protein binding; protein binding; protein homodimerization activity; receptor binding; sialic acid binding

Biological Process: brown fat cell differentiation; cellular response to insulin stimulus; fatty acid beta-oxidation; fatty acid oxidation; generation of precursor metabolites and energy; glucose homeostasis; glucose metabolic process; negative regulation of blood pressure; negative regulation of cell migration; negative regulation of fat cell differentiation; negative regulation of gluconeogenesis; negative regulation of granulocyte differentiation; negative regulation of heterotypic cell-cell adhesion; negative regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of inflammatory response; negative regulation of low-density lipoprotein receptor biosynthetic process; negative regulation of macrophage differentiation; negative regulation of MAP kinase activity; negative regulation of phagocytosis; negative regulation of protein amino acid autophosphorylation; negative regulation of smooth muscle cell migration; negative regulation of smooth muscle cell proliferation; negative regulation of synaptic transmission; negative regulation of transcription, DNA-dependent; negative regulation of tumor necrosis factor production; positive regulation of cellular protein metabolic process; positive regulation of fatty acid metabolic process; positive regulation of glucose import; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interleukin-8 production; positive regulation of myeloid cell apoptosis; positive regulation of protein amino acid phosphorylation; positive regulation of signal transduction; protein homooligomerization; regulation of fatty acid biosynthetic process; response to glucose stimulus

Disease: Adiponectin, Serum Level Of, Quantitative Trait Locus 1