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SARS virus Sm Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SARS virus Sm Antibody AP6000b
    The anti-SARS-Sm Pab (Cat. #AP6000b) is used in Western blot to detect recombinant Spike proteins, aa17-537 (Lane 1) and aa17-756 (Lane 2).
  • 产品详情
  • 文献引用 : 6
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  • 背景知识
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
WB, 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 Sm antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 532-562 amino acids from the middle of SARS CoV Spike protein.
Dilution WB~~1:1000
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 Sm Antibody 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
Mucosal immunization with surface-displayed severe acute respiratory syndrome coronavirus spike protein on Lactobacillus casei induces neutralizing antibodies in mice.
Author : Lee JS, Poo H, Han DP, Hong SP, Kim K, Cho MW, Kim E, Sung MH, Kim CJ.
J Virol. 2006 Apr;80(8):4079-87.
16571824
Coronaviral hypothetical and structural proteins were found in the intestinal surface enterocytes and pneumocytes of severe acute respiratory syndrome (SARS).
Author : Chan WS, Wu C, Chow SC, Cheung T, To KF, Leung WK, Chan PK, Lee KC, Ng HK, Au DM, Lo AW.
Mod Pathol. 2005 Nov;18(11):1432-9.
15920543
Severe acute respiratory syndrome (SARS) S protein production in plants: development of recombinant vaccine.
Author : Pogrebnyak N, Golovkin M, Andrianov V, Spitsin S, Smirnov Y, Egolf R, Koprowski H.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):9062-7. Epub 2005 Jun 14.
15956182
Severe acute respiratory syndrome coronavirus 3a protein is a viral structural protein.
Author : Ito N, Mossel EC, Narayanan K, Popov VL, Huang C, Inoue T, Peters CJ, Makino S.
J Virol. 2005 Mar;79(5):3182-6.
15709039
Resolution of primary severe acute respiratory syndrome-associated coronavirus infection requires Stat1.
Author : Hogan RJ, Gao G, Rowe T, Bell P, Flieder D, Paragas J, Kobinger GP, Wivel NA, Crystal RG, Boyer J, Feldmann H, Voss TG, Wilson JM.
J Virol. 2004 Oct;78(20):11416-21.
15452265
Synthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein.
Author : Song HC, Seo MY, Stadler K, Yoo BJ, Choo QL, Coates SR, Uematsu Y, Harada T, Greer CE, Polo JM, Pileri P, Eickmann M, Rappuoli R, Abrignani S, Houghton M, Han JH.
J Virol. 2004 Oct;78(19):10328-35.
15367599

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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