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Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Additionally we are shipping Neuraminidase, NEU Antibodies (78) and Neuraminidase, NEU Kits (16) and many more products for this protein.
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Influenza A Virus H1N1 NEU Protein expressed in Human Cells - ABIN2215932
Zhang, Xiong, Dong, Gao, Zhang, Ma, Peng, Dong, Yan: Comparison of reversed-phase liquid chromatography and hydrophilic interaction chromatography for the fingerprint analysis of Radix isatidis. in Journal of separation science 2014
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Influenza A Virus H1N1 NEU Protein expressed in Human Cells - ABIN2215929
Nair-Gupta, Baccarini, Tung, Seyffer, Florey, Huang, Banerjee, Overholtzer, Roche, Tampé, Brown, Amsen, Whiteheart, Blander: TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation. in Cell 2014
Influenza A Virus H1N1 NEU Protein expressed in Human Cells - ABIN2215934
Kim, Kim, Lee, Shin, Kim, Jung, Jeong, Hyun, Lee: Inhibition of influenza virus internalization by (-)-epigallocatechin-3-gallate. in Antiviral research 2013
Influenza A Virus H7N9 NEU Protein expressed in Human Cells - ABIN2649150
Wodal, Schwendinger, Savidis-Dacho, Crowe, Hohenadl, Fritz, Brühl, Portsmouth, Karner-Pichl, Balta, Grillberger, Kistner, Barrett, Howard: Immunogenicity and protective efficacy of a Vero cell culture-derived whole-virus H7N9 vaccine in mice and guinea pigs. in PLoS ONE 2015
Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells (By similarity).