| Description | Il1a Rat Pre-designed siRNA Set A contains three designed siRNAs for Il1a gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Il1a siRNA-1: 5 nmol (HPLC) Il1a siRNA-2: 5 nmol (HPLC) Il1a siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (Il1a Rat Pre-designed siRNA Set A contains three designed siRNAs for Il1a gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Il1a siRNA-1: 5 nmol (HPLC) Il1a siRNA-2: 5 nmol (HPLC) Il1a 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 | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard phenotype marker for the identification of T cell populations. Mature human CD4 consists of a 371 amino acid (aa) extracellular region containing four immunoglobulin-like domains, a 22 aa transmembrane segment, and a 40 aa cytoplasmic domain. Within the ECD, human CD4 shares approximately 52% aa sequence identity with mouse and rat CD4. CD4 is expressed along with CD8 on double positive T cells during their development in the thymus. Either CD4 or CD8 expression is then lost, giving rise to single positive (SP) CD4+ or CD8+ mature T cells. CD4+ SP cells, also known as T helper cells, further differentiate into multiple subsets of CD4+ cells including Th1, Th2, Th17, Tfh, and Treg cells which regulate humoral and cellular immunity. CD4 is reexpressed on circulating CD8+ T cells upon activation and contributes to their cytotoxic effector activity. In human, CD4 is additionally expressed on macrophages, neutrophils, monocytes, NK cells, and neurons and glial cells in the brain. Similar CD4 distribution between species cannot be assumed as demonstrated by its presence on macrophages in human and rat but not in mouse. CD4 binds directly to MHC class II molecules on antigen presenting cells. This interaction contributes to the formation of the immunological synapse which is focused around the TCR-MHC class II-antigenic peptide interaction. Palmitoylation of two cysteine residues in the cytoplasmic tail of CD4 promotes the localization of CD4 in lipid rafts and its ability to augment TCR signaling via activation of the tyrosine kinase Lck. CD4 also functions as a chemotactic receptor for IL-16 and, in human, as a co-receptor for the gp120 surface glycoprotein of HIV-1... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong activator of estrogen-responsive genes. ER alpha is normally quiescent and bound to heat-shock proteins and immunophilins. Following beta -estradiol binding, it becomes activated, either homodimerizes or heterodimerizes with ER beta, and binds to DNA with multiple coactivators. Human ER alpha is 595 amino acids (aa) in length. It contains a DNA binding region (aa 185-250), three NLSs (aa 256-260; 266-271; 299-303), a steroid-binding site (aa 351-543), a dimerization motif (aa 497-518), and an O-GlcNAc attachment around Thr575. Major phosphorylation sites exist at Tyr537, Ser167 and Ser118. Multiple splice forms exist. There is an 80 kDa isoform that shows a substitution (duplication) of aa 412-517 for Asp411, a second isoform with a deletion of aa 255-366, a third isoform with a deletion of aa 152-412, and a fourth isoform that shows a Thr substitution for aa 152-595. Human ER alpha is only 46% aa identical to human ER beta. Over aa 1-116, human ER alpha shares 85% aa identity with mouse ER alpha... Read More | Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionOsteoprotegerin (OPG), also named osteoclastogenesis inhibitory factor (OCIF), and tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), is a TNFRSF11B-encoded protein in humans. Acts as decoy receptor for RANKL and thereby Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionOsteoprotegerin (OPG), also named osteoclastogenesis inhibitory factor (OCIF), and tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), is a TNFRSF11B-encoded protein in humans. Acts as decoy receptor for RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local RANKL/OPG ratio. May also play a role in preventing arterial calcification. May act as decoy receptor for TRAIL and protect against apoptosis. TRAIL binding blocks the inhibition of osteoclastogenesis.OPG has been applied to decrease bone resorption in women with postmenopausal osteoporosis and in patients with lytic bone metastases... 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 |