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>   首页   >   产品   >   一抗   >   其他   >   SARS Virus SPIKE(E2GP) Antibody (C-term)   

SARS Virus SPIKE(E2GP) Antibody (C-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 P59594
Reactivity SARS
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 139125 Da
Additional info
Other Names Spike glycoprotein, S glycoprotein, E2, Peplomer protein, Spike protein S1, Spike protein S2, S
Target/Specificity This SARS Virus SPIKE(E2GP) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1226~1255 amino acids from the C-terminal region of SARS virus Spike (E2GP).
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 SPIKE(E2GP) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name S {ECO:0000255|HAMAP-Rule:MF_04099}
Function Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC- SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.
Cellular Location Virion membrane {ECO:0000255|HAMAP- Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP- Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954} Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954} Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP- Rule:MF_04099}
Research Areas

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).
Snijder, E.J., et al., J. Mol. Biol. 331(5):991-1004 (2003).
Marra, M.A., et al., Science 300(5624):1399-1404 (2003).
Krokhin, O., et al., Mol Cell Proteomics 2(5):346-356 (2003).

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