| Description | IgE is the least abundant immunoglobulin in plasma, found at a concentration of less that 0.6 micrograms/ml of normal plasma. Elevated IgE levels are found in patients experiencing severe allergic reactions and parasitic infections. In a myeloma condition, IgE is produced by a single clone of plasmaIgE is the least abundant immunoglobulin in plasma, found at a concentration of less that 0.6 micrograms/ml of normal plasma. Elevated IgE levels are found in patients experiencing severe allergic reactions and parasitic infections. In a myeloma condition, IgE is produced by a single clone of plasma cells. The structure of myeloma IgE, however, is normal, and the immunoglobulin purified from a myeloma source is a useful protein for studying immunoglobulin behavior.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.Product Citations:Janssen, Kris PF, et al. "Multiplexed protein detection using an affinity aptamer amplification assay." Analytical and bioanalytical chemistry 404, no. 6-7 (2012): 2073-2081.Schachermeyer, Samantha, et al. "Aptamer-Protein Binding Detected by Asymmetric Flow Field Flow Fractionation."Journal of Chromatography A (2013).Abe, Takaaki, et al. "Antibody against immunoglobulin E contained in blood components as causative factor for anaphylactic transfusion reactions." Transfusion (2014).Kashiwakura, Jun-ichi, et al. "Most highly cytokinergic IgEs have polyreactivity to autoantigens." Allergy, asthma & immunology research 4, no. 6 (2012): 332-340.Oh SS, et al. Synthetic aptamer-polymer hybrid constructs for programmed drug delivery into specific target cells.J Am Chem Soc. 2014 Oct 22;136(42):15010-5. doi: 10.1021/ja5079464. Epub 2014 Oct 7.Cao J, Wang H, Liu Y. Petal-like CdS nanospheres-based electrochemiluminescence aptasensor for detection of IgE with gold nanoparticles amplification. Spectrochim Acta A Mol Biomol Spectrosc. 2015;151:274-9. doi: 10.1016/j.saa.2015.06.104. Epub 2015 Jun 29.Liu YM, et al. Aptamer-based detection and quantitative analysis of human immunoglobulin E in capillary electrophoresis with chemiluminescence detection. Electrophoresis. 2015 Oct;36(19):2413-8. doi: 10.1002/elps.201500158. Epub 2015 Jul 29.Poongavanam MV, Kisley L, Kourentzi K, Landes CF, Willson RC.Ensemble and single-molecule biophysical characterization of D17.4 DNA aptamer-IgE interactions. Biochim Biophys Acta. 2016 Jan;1864(1):154-64. doi: 10.1016/j.bbapap.2015.08.008. Epub 2015 Aug 22.Garman L, Smith K, Muns EE, Velte CA, et al. Unique Inflammatory Mediators and Specific IgE Levels Distinguish Local from Systemic Reactions after Anthrax Vaccine Adsorbed Vaccination. Clin Vaccine Immunol. 2016 Aug 5;23(8):664-71. doi: 10.1128/CVI.00092-16. Print 2016 Aug.Ref:Ishiaka, K.1985. Methods Enzymol. 116, 76... Read More | Usually used industrially for the resolution of chiral compounds and the transesterification production of biodiesel | N-Acetylneuraminyl-fucosyllacto-N-neo-tetraose is used as a reference material in the analysis of milk oligosaccharides | Store at -20°C. Store under desiccating conditions. The product can be stored for up to 12 months | 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 |