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SARS-ACSMS(C) (residues 1051-1076/1121-1154/1162-1190)

SARS-Associated Coronavirus Spike Mosaic S(C)

recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-1105 100 μg 234,90 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on gel packs

Storage Conditions: store at -20 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 37 kDa

Purity: > 95 % (SDS-PAGE)

Form: liquid (Supplied in 25 mM Tris-HCl, 0.4% sarcosyl, 0,25% Triton X-100 and 50% glycerol)

Recombinant SARS-ACSM Antigen may be used in ELISA and Western blots, excellent for detection of SARS with minimal specificity problems.

SARS-ACSM contains the C-terminal t section of the Spike protein immunodominant fragments, amino acids: 1051-1076, 1121-1154, 1162-1190. SARS-ACSM is purified by proprietary chromatographic techniques.

Background: The spike (S) glycoprotein of coronaviruses mediates viral entry into host cells. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. It is a type 1 viral fusion protein that characteristically contains two heptad repeat regions, denoted HR-N and HR-C, that form coiled-coil structures within the ectodomain of the protein. Previous studies have shown that the two heptad repeat regions can undergo a conformational change from their native state to a 6-helix bundle (trimer of dimers), which mediates fusion of viral and host cell membranes.

Specificity: Immunoreactive with sera of SARSinfected individuals.

BIOZ Product Citations:
Please click the arrow on the right to expand the citation list. Click publication title for the full text.

Selected References:
Xu et al. (2004) Characterization of the heptad repeat regions, HR1 and HR2, and design of a fusion core structure model of the spike protein from severe acute respiratory syndrome (SARS) coronavirus. Biochemistry 43:14064.
Hsu et al. (2004) Immunological, structural, and preliminary Xray diffraction characterizations of the fusion core of the SARScoronavirus spike protein. Biochem. Biophys. Res. Commun. 324:761.
He et al. (2004) Identification of immunodominant sites on the spike protein of severe acute respiratory syndrome (SARS) coronavirus: implication for developing SARS diagnostics and vaccines. J. Immunol. 173:4050.
Bukreyev et al. (2004) Mucosal immunisation of African green monkeys (Cercopithecus aethiops) with an attenuated parainfluenza virus expressing the SARS coronavirus spike protein for the prevention of SARS. Lancet. 363:2122.
Hua et al. (2004) Identification of two antigenic epitopes on SARS-CoV spike protein. Biochem. Biophys. Res. Commun. 319:929.
Bosch et al. (2004) Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Proc. Natl. Acad. Sci. USA. 101:8455.