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Follow on Google News | Cholesterol removal from serum samples using Cleanascite™ for vaccine researchCholesterol removal from serum samples using Cleanascite™ for immunogenicity and safety endpoint analysis of pneumococcal pneumolysin derivative PlyD1 in a single-antigen protein vaccine.
For detailed protocols of the published article click http://www.sciencedirect.com/ Characteristics Of Cleanascite™ Does not bind to DNA, RNA, enzymes and proteins Leaves glycoproteins, antibodies, nucleic acids, hemoglobin, proteoglycans, nucleic acids, serum components(such as hormones, nutrients, globulins, clotting factors, transport proteins) alone Extends the life of membrane and chromatographic columns. Ideal for delipidation treatments for downstream processing of large-scale therapeutic proteins, enzymes and monclonal antibodies. Ideal for clarifying ascites, serum, cell & tissue culture, bile and organ homogenates For more information, visit: Cleanascite™ http://www.biotechsupportgroup.com/ About Biotech Support Group LLC Biotech Support Group LLC is a leading provider of genomics and proteomics sample preparation products and enrichment reagent kits as well as integrated biotechnology services for life sciences research, biomarker and drug discovery. Based in New Jersey, it’s principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ CONTACT: Dr.Swapan Roy Biotech Support Group 1 Deer Park Drive, Suite M, Monmouth Junction, NJ 08852, USA 732-274-2866 sales@biotechsupportgroup.com Cleanascite™ Plasma/Serum Kamtchoua, Thierry, Monica Bologa, Robert Hopfer, David Neveu, Branda Hu, Xiaohua Sheng, Nicolas Corde, Catherine Pouzet, Gloria Zimmerman, and Sanjay Gurunathan. "Safety and immunogenicity of the pneumococcal pneumolysin derivative PlyD1 in a single-antigen protein vaccine candidate in adults." Vaccine (2012). http://www.sciencedirect.com/ Lijowski M, Caruthers S, Hu G. High-Resolution SPECT-CT/MR Molecular Imaging of Angiogenesis in the Vx2 Model Investigative Radiology.2009; Turner JD, Langley RS, Johnston KL. Wolbachia Lipoprotein Stimulates Innate and Adaptive Immunity through Toll-like Receptors 2 and 6 to Induce Disease Manifestations of Filariasis The Journal of Biological Chemistry.2009; http://www.jbc.org/ Torrelles JB, DesJardin LE, MacNeil J. et al Inactivation of Mycobacterium tuberculosis mannosyltransferase pimB reduces the cell wall lipoarabinomannan and lipomannan content and increases the rate of bacterial-induced human macrophage cell death Glycobiology.2009; http://glycob.oxfordjournals.org/ Cho N, Chueh PJ, Kim C et al Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone (NADH) oxidase from the sera of cancer patients. Cancer Immunology, Immunotherapy. 2002;51(3):121- http://www.springerlink.com/ Shapiro S, Beenhouwer DO, Feldmesser M et al. Immunoglobulin G Monoclonal Antibodies to Cryptococcus neoformans Protect Mice Deficient in Complement Component C3 Infect. Infection and immunity.2002; http://iai.asm.org/ Castro AR, Morrill We, Pope V. Lipid Removal from Human Serum Samples Clinical and diagnostic laboratory immunology.2000; http://www.ncbi.nlm.nih.gov/ Nussbaum G, Cleare W, Casadevall A et al Epitope Location in the Cryptococcus neoformans Capsule Is a Determinant of Antibody Efficacy The Journal of experimental medicine.1997; http://jem.rupress.org/ Suggested References Salha, Danielle, et al. "Neutralizing Antibodies Elicited by a Novel Detoxified Pneumolysin Derivative, PlyD1, Provide Protection against Both Pneumococcal Infection and Lung Injury." Infection and immunity 80.6 (2012): 2212-2220. http://iai.asm.org/ Pichichero, Michael E., et al. "Antibody response to Streptococcus pneumoniae proteins PhtD, LytB, PcpA, PhtE and Ply after nasopharyngeal colonization and acute otitis media in children." Human Vaccines & Immunotherapeutics 8.6 (2012): 799-805. http://www.es.landesbioscience.com/ Ljutic, Belma, et al. "Formulation, stability and immunogenicity of a trivalent pneumococcal protein vaccine formulated with aluminum salt adjuvants."Vaccine (2012). http://www.sciencedirect.com/ Alexander, Janet E., et al. "Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae." http://iai.asm.org/ Berry, A. M., J. Yother, D. E. Briles, D. Hansman, and J. C. Paton. "Reduced virulence of a defined pneumolysin- http://iai.asm.org/ Tilley, Sarah J., et al. "Structural basis of pore formation by the bacterial toxin pneumolysin." http://www.sciencedirect.com/ Mitchell, T. J., et al. "Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute‐phase protein." Molecular microbiology 5.8 (2006): 1883-1888. http://onlinelibrary.wiley.com/ Paton, James C. "The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniae." http://www.sciencedirect.com/ Boulnois, G. J., J. C. Paton, T. J. Mitchell, and P. W. Andrew. "Structure and function of pneumolysin, the multifunctional, thiol‐activated toxin of Streptococcus pneumoniae." http://onlinelibrary.wiley.com/ Nöllmann, Marcelo, et al. "The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin." Biophysical journal 86.5 (2004): 3141-3151. http://www.sciencedirect.com/ End
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