Key features and details
- Expression system: Escherichia coli
- Purity: > 98% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant mouse Adiponectin protein (Globular Domain)
See all Adiponectin proteins and peptides
Determined by its ability to inhibit the proliferation of murine myeloid cell lines M1. The ED50 for this effect is ≤ 15 µg/ml.
Purity> 98 % SDS-PAGE.
SDS-PAGE & HPLC analysis
Endotoxin level< 1.000 Eu/µg
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMKGEPGEAAYMYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGK FYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASG SVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN
Predicted molecular weight17 kDa
Our Abpromise guarantee covers the use of ab54483 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signalling muscle to absorb and burn Free-Fatty Acids (FFAs). The signalling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant mouse gAcrp30 (ab54483) is a 16.6 kDa protein consisting of 145 amino acid residues.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ReconstitutionReconstitute in water to a concentration of 0.1-1.0mg/ml. This solution can be diluted in water or other buffer solutions.
- 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.
ab54483 has been referenced in 1 publication.
- Yang L et al. Expression of apolipoprotein M and its association with adiponectin in an obese mouse model. Exp Ther Med 18:1685-1692 (2019). PubMed: 31410126