| Description | KYNU Human Pre-designed siRNA Set A contains three designed siRNAs for KYNU gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KYNU siRNA-1: 5 nmol (HPLC) KYNU siRNA-2: 5 nmol (HPLC) KYNU siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 KYNU Human Pre-designed siRNA Set A contains three designed siRNAs for KYNU gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KYNU siRNA-1: 5 nmol (HPLC) KYNU siRNA-2: 5 nmol (HPLC) KYNU siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Inquire | Purity＞95% SDS-PAGE.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 Purity＞95% SDS-PAGE.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.Post-translationalHydroxylated 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... Read More | Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals... Read More | Inquire |