| Description | CFLAR Human Pre-designed siRNA Set A contains three designed siRNAs for CFLAR gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CFLAR siRNA-1: 5 nmol (HPLC) CFLAR siRNA-2: 5 nmol (HPLC) CFLAR siRNA-3: 5 nmol (HPLC) siRNA Negative Control:CFLAR Human Pre-designed siRNA Set A contains three designed siRNAs for CFLAR gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CFLAR siRNA-1: 5 nmol (HPLC) CFLAR siRNA-2: 5 nmol (HPLC) CFLAR 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 | Store at +4°C. Store under desiccating conditions. The product can be stored for up to 12 months | PTD-p65-P1 Peptide TFA is a potent, selective nuclear transcription factor NF-κB inhibitor and derives from the p65 subunit of NF-κB amino acid residues 271-282, which selectively inhibits NF-κB activation induced by various inflammatory stimulation, downAppearance:SolidIC50& PTD-p65-P1 Peptide TFA is a potent, selective nuclear transcription factor NF-κB inhibitor and derives from the p65 subunit of NF-κB amino acid residues 271-282, which selectively inhibits NF-κB activation induced by various inflammatory stimulation, downAppearance:SolidIC50& Target:NF-kappaBIn Vitro:PTD-p65-P1 Peptide TFA (10-150 µM; 0-60 min; KBM-5 cells) inhibits TNF-induced NF-κB activation in a dose-dependent manner and suppresses TNF-induced NF-κB activation by 25% at 100 µM and completely at 150 µM. PTD-p65-P1 Peptide TFA (150 µM; 0-60 minBiological Activity:PTD-p65-P1 Peptide TFA is a potent, selective nuclear transcription factor NF-κB inhibitor and derives from the p65 subunit of NF-κB amino acid residues 271-282, which selectively inhibits NF-κB activation induced by various inflammatory stimulation, down... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |