| Description | KIRREL1 Human Pre-designed siRNA Set A contains three designed siRNAs for KIRREL1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KIRREL1 siRNA-1: 5 nmol (HPLC) KIRREL1 siRNA-2: 5 nmol (HPLC) KIRREL1 siRNA-3: 5 nmol (HPLC) siRNA KIRREL1 Human Pre-designed siRNA Set A contains three designed siRNAs for KIRREL1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KIRREL1 siRNA-1: 5 nmol (HPLC) KIRREL1 siRNA-2: 5 nmol (HPLC) KIRREL1 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 | Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Receptor-1, PAR-1 Agonist induces activation of protein kinase C isoenzymes alpha and epsilon in human HT-29 colon carcinoma cells expressing PAR1 endogeneously. On the cellular level, Protease-Activated Receptor-1, PAR-1 Agonist and thrombin prompted HT-29 cell migration and matrix adhesion by a PKCepsilon-dependent mechanism as concluded because of the inhibition of PAR1-mediated effects by the PKC inhibitor bisindolylmaleimide I and the PKCepsilon translocation inhibitory peptide EAVSLKPT but not by the PKC inhibitor Gö 6976. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:PAR-1... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 amino acid (aa) precursor that includes a 28 aa signal sequence, a 215 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 61 aa cytoplasmic domain. The ECD is composed of one Ig-like V-type domain and one Ig-like C2-type domain. Within the ECD, human CD200 R1 shares 56% aa sequence identity with both mouse and rat CD200 R1. Alternate splicing of the human CD200 R1 mRNA generates four isoforms, two of which are truncated in the Ig-C2 domain and are likely secreted. In human, a separate CD200 RL gene encodes a protein that shares 81% ECD aa identity with CD200 R1. In mouse, at least four genes for CD200 R1-like molecules have been described. CD200 R1 expression is restricted primarily to mast cells, basophils, macrophages, and dendritic cells, while its ligand, CD200, is widely distributed. Disruption of this receptor-ligand system by knockout of the CD200 gene in mice leads to increased macrophage number and activation and predisposition to autoimmune disorders. Association of CD200 with CD200 R1 takes place between their respective N-terminal Ig-like domains. The capacity of CD200 R1-like molecules to interact with CD200 is controversial. CD200 R1 propagates inhibitory signals despite lacking a cytoplasmic ITIM (immunoreceptor tyrosine-based inhibitory motif). CD200 R1-like molecules, in contrast, are potentially activating receptors by means of their association with DAP12. CD200R1 signaling inhibits the expression of proinflammatory molecules including TNFs, IFNs, and inducible nitric oxide synthase in response to selected stimuli, which implicate that CD200/CD200R1 inhibitory signaling pathway plays a prominent role in limiting inflammation in a wide range of inflammatory diseases. Furthermore, the CD200/CD200R inhibitory signaling constitutes one of the most suitable endogenous immunoregulatory molecule candidate to restore the immune suppressive status of the CNS altered in chronic neuroinflammatory situations... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems... 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 |