Technical Data
SARS E Protein (NT) (Severe Acute Respiratory Syndrome)
A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive stranded RNA approximately 27 to 31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139kD protein and the major surface antigen of the virus, to the angiotensin converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. 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.
PabAffinity Purified
100ug-20CBlue IceRabbit
As reported
Synthetic peptide corresponding to amino acids at the N-terminus of the SARS E protein.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, 0.02% sodium azide.
Recognizes SARS-Associated Coronavirus (SARS-CoV) E protein (N-terminal)
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Marra, MA., et al., (2003), "The Genome sequence of the SARS-associated corona virus", Science, 300, 1399-1404. 2. Rota, P.A., et al., (2003), "Characterization of a novel coronavirus associated with severe acute respiratory syndrome", Science, 300, 1394-1399. 3. Navas-Martin, S.R., et al., (2004), Coronavirus replication and pathogenesis: Implications for the recent outbreak of severe acute respiratory syndrome (SARS), and the challenge for vaccine development", J. Neurovirol., 10, 75-85. 4. Arbely, E., et al., (2004), "A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E Protein", J. Mol. Biol., 3414, 769-779. 5. Maeda, J. et al., (1999), "Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells", Virology, 263, 265-272.