SARS, Spike Protein, Mosaic (N), Recombinant (aa12-53, 90-115, 171-203) (Severe Acute Respiratory Syndrome, SARS-CoV, SARS Associated Coronavirus)

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\n\nSARS-ACSM contains the middle section of the Spike protein immunodominant regions, amino acid fragments: (12-53), (90-115), (171-203).\n\nSpecificity:\nImmunoreactive with sera of SARS-infected individuals\n\nApplication:\nRecombinant SARS-ACSM Antigen may be used in ELISA and Western Blot, excellent for detection of SARS with minimal specificity problems.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S0098-17D

Size

100ug

Form

Supplied as a liquid in 50mM Tris-HCl, 60mM sodium chloride and 50% glycerol.

Purity

(same/more than) 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.

References

1. 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. Xu Y, Zhu J, Lou Z, Ni L, Gao GF, Biochemistry 2004 Nov 9;43(44):14064-71 2. Immunological, structural, and preliminary X-ray diffraction characterizations of the fusion core of the SARS-coronavirus spike protein. Hsu CH, Ko TP, Tang TK, Biochem Biophys Res Commun 2004 Nov 12;324(2):761-7 3. Identification of immunodominant sites on the spike protein of severe acute respiratory syndrome (SARS) coronavirus: implication for developing SARS diagnostics and vaccines. He Y, Zhou Y, Luo B, J Immunol 2004 Sep 15;173(6):4050-7 4. Mucosal immunisation of African green monkeys (Cercopithecus aethiops) with an attenuated parainfluenza virus expressing the SARS coronavirus spike protein for the prevention of SARS. Bukreyev A, Lamirande EW, Vogel LN, Subbarao K, Lancet 2004 Jun 26;363(9427):2122-7 5. Identification of two antigenic epitopes on SARS-CoV spike protein. Hua R, Zhou Y, Hua Y, Biochem Biophys Res Commun 2004 Jul 2;319(3):929-35 6. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Bosch BJ, Martina BE, Lepault J, De Groot R, Proc Natl Acad Sci U S A 2004 Jun 1;101(22):8455-60.