Key features and details
- Expression system: Escherichia coli
- Purity: >= 98% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Active: Yes
Product nameRecombinant mouse Adiponectin protein (Active)
See all Adiponectin proteins and peptides
Determined by its ability to inhibit the proliferation of murine myeloid cell lines M1. The ED50 for the effect is < 15 µg/ml.
Purity>= 98 % SDS-PAGE.
Endotoxin level< 1.000 Eu/µg
Expression systemEscherichia coli
Protein lengthFull length protein
Predicted molecular weight17 kDa
Our Abpromise guarantee covers the use of ab285603 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This product is manufactured by BioVision, an Abcam company and was previously called 4592 gAcrp30/Adiponectin, murine recombinant. 4592-100 is the same size as the 100 µg size of ab285603.
Centrifuge the vial prior to opening.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C. Store under desiccating conditions.
Constituent: 0.061% Tris
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ReconstitutionReconstitute in 5 mM Tris, pH 7.6 to a concentration of 0.1-1.0 mg/ml. This stock solution can then be diluted into other aqueous buffers
- 30 kDa adipocyte complement related protein
- 30 kDa adipocyte complement-related protein
FunctionImportant 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.
Tissue specificitySynthesized exclusively by adipocytes and secreted into plasma.
Involvement in diseaseDefects 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.
Sequence similaritiesContains 1 C1q domain.
Contains 1 collagen-like domain.
DomainThe C1q domain is commonly called the globular domain.
modificationsHydroxylated 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.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab285603 has not yet been referenced specifically in any publications.