Adiponectin/Acrp30 Polyclonal Antibody(Capture/Detector)
Price:
- 宿主： Rabbit
- 反应性： Rat
- 应用性： ELISA Capture/Detector
| Verified Samples |
Verified Samples in ELISA: Recombinant Rat Adiponectin/Acrp30 protein, Rat serum, Rat plasma |
| Dilution | ELISA Capture 2-8 μg/mL, ELISA Detector 0.1-0.4 μg/mL |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Immunogen | Recombinant Rat Adiponectin/Acrp30 protein expressed by E.coli |
| Abbre | Adiponectin/Acrp30 |
| Synonyms | Acrp30, Adipoq, Adid, 30 kDa adipocyte compLement-reLated protein, Adiponectin d, Adiponectin, C1Q and coLLagen domain containing |
| Swissprot | |
| Concentration | 1 mg/mL |
| Storage | Store at 4°C valid for 12 months or -20°C valid for long term storage, avoid freeze / thaw cycles. |
| Buffer | Phosphate buffered solution, pH 7.2, containing 0.05% proclin 300. |
| Purification Method | Antigen Affinity Purification |
| Conjugation | Unconjugated |
| Background | Adiponectin,alternately named Adipocyte complement-related protein of 30 kDa (Acrp30),adipoQ,adipose most abundant gene transcript 1 (apM1),and gelatin-binding protein of 28 kDa (GBP28),is an adipocyte-specific,secreted protein with potential roles in glucose and lipid homeostasis. Circulating Adiponectin levels are high,accounting for approximately 0.01% of total plasma protein. Adiponectin contains a modular structure that includes an N-terminal collagen-like domain followed by a C-terminal globular domain with significant sequence and structural resemblance to the complement factor C1q. Although they share little sequence identity,similar threedimensional structure and certain conserved amino acid residues suggest an evolutionary link between the C1q-like domain of Adiponectin and members of the TNF superfamily. Adiponectin assembles into different complexes including trimers (low molecular weight),hexamers (middle molecular weight),and higher order oligomeric structures (high molecular weight) that may affect biological activity. Adiponectin is induced during adipocyte differentiation and its secretion is stimulated by insulin. Two receptors for Adiponectin,termed AdipoR1 and AdipoR2,have been cloned. Although functionally distinct from G-protein-coupled receptors,the genes encode predicted proteins containing 7 transmembrane domains. AdipoR1 is highly expressed in skeletal muscle,while AdipoR2 is primarily found in hepatic tissues. |
