Technical Data
S0098-41C
SARS M Protein, CT (Severe Acute Respiratory Syndrome)
Description:
SARS (Severe acute respiratory syndrome) Membrane glycoprotein, also known as M protein or Matrix protein. This protein is predicted to contain a triple-spanning transmembrane region, a small external N-terminal domain and a longer C-terminal region in the interior. SARS Membrane Protein is the major component of the virion envelope, and has an important structural role. The protein is also believed to interact with the Spike and Nucleocapsid proteins along with participating in virion assembly.

Applications:
Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 1.0ug/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.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceRabbit
Concentration:
As reported
Immunogen:
Synthetic peptide corresponding to sequence from the carboxy terminus of SARS Membrane Protein.
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS, 0.02% sodium azide.
Specificity:
Recognizes SARS (Severe acute respiratory syndrome) Membrane glycoprotein.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Marra, M.A., et al (2003) The Genome sequence of the SARS-associated corona virus. Science 300:1399-404. 2. Rota, P.A., et al (2003) Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 300:1394-9. 3. Navas-Martin, S.R., (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. Opstelten, D.J., et al (1995) Envelope glycoprotein interactions in coronavirus assembly. J Cell Biol. 131:339-49.