Adiponectin (GWB-842BE5)



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Sequence: MGHDQETTTQ GPGVLLPLPK GACTGWMAGI PGHPGHNGAP GRDGRDGTPG EKGEKGDPGL IGPKGDIGET GVPGAEGPRG FPGIQGRKGE PGEGAYVYRS AFSVGLETYV TIPNMPIRFT KIFYNQQNHY DGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HLEVGDQVWL QVYGEGERNG LYADNDNDST FTGFLLYHDT N Concentration: Lot specific and is stated on the vial. Human Adiponectin, also referred to as AdipoQ, Acrp30, apm-1 or GBP28, is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia. Recombinant human Adiponectin protein was expressed in Ecoli and purified by conventional chromatography, after refolding of the isolated inclusion bodies in a renaturation buffer.

Function: 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.

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: 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.

Ptm: 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).

Ptm: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.

Ptm: Not N-glycosylated.

Disease: 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.

Pharmaceutical: Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.

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.

Miscellaneous: 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.

Similarity: Contains 1 C1q domain.

Similarity: Contains 1 collagen-like domain. 1. Maeda K., et al. (1996) Biochem Biophys Res Commun. 221:286-9.
1. Berg AH., et al. (2001) Nat Med; 7:947-53
1. Berg AH., et al. (2002) Trends Endocrinol Metab. 13: 84-89.
1. Yamauchi T et al., (2002) Nat Med. 8:1288-95

Additional Information

Name Adiponectin (GWB-842BE5)
Availability In Stock
Related Product Names Adiponectin Human, Recombinant, E Coli; Adipocyte, C1q and collagen domain-containing protein; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipose most abundant gene transcript 1 protein; apM-1; Gelati
Swissprot ID Q15848
NCBI Acc Number NP_004788.1
Molecular Weight 25.1 kDa (231 aa
Purity >= 90% by SDS PAGE
Format Liquid. In PBS, pH 7.4 containing 1 mM DTT
Storage Can be stored at 4C short term (1-2 weeks). For long term storage, aliquot store at -20C or -70C. Avoid repeated freezing and thawing cycles.
Datasheets/Manuals Printable datasheet for GWB-842BE5
Intended Use Research Use Only