SARS virus PUPM Antibody (C-term)

日期:2020-08-01 00:36 人气:
Catalog_no AB2362
Product_name SARS virus PUPM Antibody (C-term)
Category 抗原抗体
Reactivity S
Size 100μL/50μL
Price 2000.00/1100.00
immunogen CVHSA:192-221
Specificity This SARS virus PUPM antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 192~221 amino acids from the C-terminus region of SARS M protein.
Purification Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
othername Membrane protein, M protein, E1 glycoprotein, Matrix glycoprotein, Membrane glycoprotein, M
Isotype Rabbit Ig
Background An outbreak of atypical pneumonia, referred to as severe acute respiratory syndrome (SARS) and first identified in Guangdong Province, China, has spread to several countries. The severity of this disease is such that the mortality rate appears to be ~3 to 6%. A number of laboratories worldwidehave undertaken the identification of the causative agent. The National Microbiology Laboratory in Canada obtained the Tor2 isolate from a patient in Toronto, and succeeded in growing a coronavirus-like agent in African Green Monkey Kidney (Vero E6) cells. This coronavirus has been named publicly by the World Health Organization and member laboratories as ?SARS virus? The SARS membrane proteins, including the major proteins S (Spike) and M (Membrane), are inserted into the endoplasmic reticulum Golgi intermediate compartment (ERGIC) while full length replicated RNA (+ strands) assemble with the N (nucleocapsid) protein. The virus then migrates through the Golgi complex and eventually exits the cell, likely by exocytosis. The site of viral attachment to the host cell resides within the S protein. Oligomeric spike (S) glycoproteins extend from SARS membranes. These integral membrane proteins assemble within the endoplasmic reticulum of infected cells and are subsequently endoproteolyzed in the Golgi, generating noncovalently associated S1 and S2 fragments. Once on the surface of infected cells and virions, peripheral S1 fragments bind carcinoembryonic antigen-related cell adhesion molecule (CEACAM) receptors, and this triggers membrane fusion reactions mediated by integral membrane S2 fragments.
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