Rabbit Anti-SARS-CoV Membrane Protein Polyclonal antibody for IF, WB, IP. SARS-CoV membraneprotein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoVmembraneprotein in the stacking gels, results in the failure to detect the membraneprotein in the separating gels. Aggregated membraneproteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoVmembraneprotein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from247to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoVmembraneprotein is not unique among structural proteins of coronaviruses. However, SARS-CoVmembraneprotein seems to be more sensitive to heat treatment, since the membraneprotein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoVmembraneprotein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoVmembraneprotein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoVmembraneprotein aggregation induced by heat also provides a model for the study of protein aggregation.
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