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>   首页   >   产品   >   一抗   >   微生物学   >   SARS virus PUPM Antibody (N-term)   

SARS virus PUPM Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
E
Primary Accession P59596
Reactivity SARS
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 25061 Da
Additional info
Gene ID 1489672
Other Names Membrane protein, M protein, E1 glycoprotein, Matrix glycoprotein, Membrane glycoprotein, M
Target/Specificity This SARS virus PUPM antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1~30 amino acids from the N-terminus region of SARS M protein.
Format 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.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsSARS virus PUPM Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name M {ECO:0000255|HAMAP-Rule:MF_04202}
Function Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Cellular Location Virion membrane {ECO:0000255|HAMAP- Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP- Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04202}. Note=Largely embedded in the lipid bilayer {ECO:0000255|HAMAP-Rule:MF_04202}
Research Areas
Chimeric coronavirus-like particles carrying severe acute respiratory syndrome coronavirus (SCoV) S protein protect mice against challenge with SCoV.
Author : Lokugamage KG1,Yoshikawa-Iwata N,Ito N,Watts DM,Wyde PR,Wang N,Newman P,Kent Tseng CT,Peters CJ,Makino S.
Vaccine. 2008 Feb 6;26(6):797-808. doi: 10.1016/j.vaccine.2007.11.092. Epub 2007 Dec 26.
18191004

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.

REFERENCES

He, R., et al., Biochem. Biophys. Res. Commun. 316(2):476-483 (2004).
Zhang, X.L., et al., Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35(12):1140-1144 (2003).
Snijder, E.J., et al., J. Mol. Biol. 331(5):991-1004 (2003).
Marra, M.A., et al., Science 300(5624):1399-1404 (2003).

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