Anti-Adiponectin Antibody - BSA and Azide free (Capture) (RMAB-0252352)
Cat. No.: RMAB-0252352
Category: Antibody Pair
INQUIRY
100 μg
1 mg
Rabbit monoclonal to Adiponectin - BSA and Azide free (Capture)
Product Features
| Isotype | IgG |
|---|---|
| Clonality | Monoclonal |
| Host Species | Rabbit |
| Clone Number | EPR21976-282 |
| Form | Liquid |
| Species Reactivity | Rat |
| Applications | Sandwich ELISA |
| Key Features | Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply; Rabbit monoclonal to Adiponectin - BSA and Azide free (Capture); Suitable for: Sandwich ELISA; Reacts with: Rat |
Target Information
| Target Symbol | ADIPOQ |
|---|---|
| Target Name | Adiponectin |
| UniProt ID | Q15848 |
| Cellular Localization | Secreted. |
| 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. |
| Involvement in Disease | Defects in ADIPOQ are the cause of adiponectin deficiency (ADPND). ADPND results in very low concentrations of plasma adiponectin.Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM); also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance. |
| Post-translational Modifications | 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. |
| Domain | The C1q domain is commonly called the globular domain. |
| Sequence Similarities | Contains 1 C1q domain. Contains 1 collagen-like domain. |
Storage & Shipping
| Storage Buffer | Constituent: 100% PBS |
|---|---|
| Storage & Shipping | Shipped at 4°C. Store at 4°C. |
For research use only. Not for clinical use.
