| Description | Buy Purified Native Angiotensinogen from Human Plasma direct from the manufacturer.Bulk Qty Available.Angiotensinogen (AGT) is a glycoprotein found in plasma at a concentration of 2.8-7.1 mg per 100mL in healthy individuals. AGT is produced primarily by the liver but also is synthesized in the brainBuy Purified Native Angiotensinogen from Human Plasma direct from the manufacturer.Bulk Qty Available.Angiotensinogen (AGT) is a glycoprotein found in plasma at a concentration of 2.8-7.1 mg per 100mL in healthy individuals. AGT is produced primarily by the liver but also is synthesized in the brain, large arteries, kidneys and adipose tissue. In plasma it exists as a monomeric form (55-65 kDa) as well as a high molecular mass form (200-550 kDa). In non-pregnant individuals with normal blood pressure, the high molecular mass form accounts for 3% of total circulating AGT. In the first half of pregnancy the total AGT increases by 4-fold and the high molecular mass form increases by 20-fold. Up to 80% of the total AGT in amniotic fluid is the high molecular mass form.Angiotensinogen is an essential component of the renin-angiotensin system, a potent regulator of blood pressure, body fluid and electrolyte homeostasis. It functions as the substrate for human renin and is the precursor molecule for Angiotensins 1,2,3,4, 1-9, 1-7, 1-5 and 1-4. AGT is also a member of the SERPIN family but it is not known to possess protease-inhibitory activity. Levels in plasma are increased by plasma corticosteroid, estrogen, thyroid hormone and angiotensin-2 levels. Synonym: Hypertensinogen, Renin substratePrepared from plasma shown to be non-reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests... Read More | Inquire | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... Read More | 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 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 |