Technical Data
SARS M Protein (NT) (Severe Acute Respiratory Syndrome, Matrix Glycoprotein)
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 27-31kb in length. The M protein (Membrane protein, Matrix protein) is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein and the nucleocapsid protein.

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.
PabIgGAffinity Purified
100ug-20CBlue IceRabbit
As reported
Synthetic peptide corresponding to amino acids at the N-terminus of the SARS M protein.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, 0.02% sodium azide.
Recognizes the N-terminal of the M protein of SARS-associated coronavirus.
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.