| 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 | Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using liquid chromatography?mass spectrometry (LC-MS)/MS. It has also been used for liposome preparation... Read More | Inquire | Inquire | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More |