The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
The cystenine 39 was replaced with alanine (C39A)9. mAd-C39A can only form trimer, but not hexamer or HMW form.
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Shipped at 4°C. Store at -20ºC.
Add 100µl of deionized water to prepare a working stock solution of
approximately 1 mg/mL and let the lyophilized pellet dissolve completely.
Product is not sterile, please filter the product by an appropriate sterile filter before using it in cell culture. Aliquot reconstituted protein and avoid repeated freezing/thawing cycles and store at –80°C for long term storage.
30 kDa adipocyte complement related protein
30 kDa adipocyte complement-related protein
Adipocyte C1q and collagen domain containing protein
Adipocyte complement related 30 kDa protein
Adipocyte complement related protein of 30 kDa
Adipocyte complement-related 30 kDa protein
adipocyte-specific secretory protein
adiponectin, C1Q and collagen domain containing
Adipose most abundant gene transcript 1
Adipose most abundant gene transcript 1 protein
Adipose specific collagen like factor
C1q and collagen domain-containing protein
Gelatin binding protein
Gelatin binding protein 28
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.
Synthesized exclusively by adipocytes and secreted into plasma.
Defects in ADIPOQ are the cause of adiponectin deficiency (ADPND) [MIM:612556]. ADPND results in very low concentrations of plasma adiponectin. Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance.
The C1q domain is commonly called the globular domain.
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. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation.