金山科研平台，产品价格货期咨询微信：jinshanbio Source:Mouse myeloma cell line, NS0-derived, Ser37-Lys449, with an N-terminal vasodilator-stimulated phosphoprotein tetramerization domain and a C-terminal 6-His tag Accession #:Q6DPL2 N-terminal Sequence Analysis:Ser (tetramerization domain) Purity:>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 µg per lane. Predicted Molecular Mass:51kDa SDS-PAGE:58-65 kDa, reducing conditions Activity:Measured by its ability to cleave a fluorogenic substrate, 2’-(4-Methylumbelliferyl)-alpha -D-N-acetylneuraminic acid. The specific activity is >2,500 pmol/min/µg, as measured under the described conditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris, NaCl and Glycerol.See Certificate of Analysis for details. Molecule Information: Viral Neuraminidase Aliases: NANH Background: Neuraminidases Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of influenza virus. HA is a lectin that binds sialic acid on host cell membrane. Neuraminidase is a sialic acid hydrolase that specifically clips off terminally located sialic acid on host cell surface. The two proteins are essential for infectious cycle of influenza virus. During initial infection, an influenza virus will hold onto an epithelial cell through HA-sialic acid interaction. At the end of an infectious cycle, the neuraminidase will cleave the sialic acid on the host cell membrane, releasing the newly formed viral particle from the HA-sialic acid bondage. The neuraminidase activity is also thought to help the virus penetrate mucus. Nine subtypes of NA have been identified, all of which are tetrameric and share a common structure consisting of a globular head, a thin stalk region, and a small hydrophobic region that anchors the protein in the virus membrane.