Human Adiponectin/Acrp30 protein (Recombinant) (His-Tag) (STJP018738)
SPECIFICATIONS
HostE.coli
ImmunogenHuman
General Information
| Short Description | Recombinant-Human Adiponectin/Acrp30-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | SDS-PAGE/Denatured |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 1 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol, 0.4M urea |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | ADIPOQ |
| Gene ID | 9370 |
| Uniprot ID | ADIPO_HUMAN |
| Accession Number | NP_004788 |
| Immunogen | Human |
| Immunogen Region | 108-244aa |
| Immunogen Sequence |
Additional Info
| Tissue Specificity | Synthesized exclusively by adipocytes and secreted into plasma. |
| Post Translational Modifications | HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-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. Succination of Cys-36 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits polymerization and secretion of adiponectin. Adiponectin is a major target for succination in both adipocytes and adipose tissue of diabetic mammals. It was proposed that succination of proteins is a biomarker of mitochondrial stress and accumulation of Krebs cycle intermediates in adipose tissue in diabetes and that succination of adiponectin may contribute to the decrease in plasma adiponectin in diabetes. |
| 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. |
| Protein Name | Adiponectin30 Kda Adipocyte Complement-Related ProteinAdipocyte Complement-Related 30 Kda ProteinAcrp30Adipocyte - C1q And Collagen Domain-Containing ProteinAdipose Most Abundant Gene Transcript 1 ProteinApm-1Gelatin-Binding Protein |
| Database Links | Reactome: R-HSA-163680Reactome: R-HSA-381340Reactome: R-HSA-9841922 |
| Cellular Localisation | Secreted |
| Alternative Protein Names | Adiponectin protein30 Kda Adipocyte Complement-Related Protein proteinAdipocyte Complement-Related 30 Kda Protein proteinAcrp30 proteinAdipocyte - C1q And Collagen Domain-Containing Protein proteinAdipose Most Abundant Gene Transcript 1 Protein proteinApm-1 proteinGelatin-Binding Protein proteinADIPOQ proteinACDC proteinACRP30 proteinAPM1 proteinGBP28 protein |
Information sourced from Uniprot.org