The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity70 - 90% by HPLC.
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions. - If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer. - Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent. - Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised. - Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Information available upon request.
DEAD (Asp Glu Ala Asp) box polypeptide 58
DEAD (Asp Glu Ala Asp/His) box polypeptide
DEAD box protein 58
DEAD/H (Asp Glu Ala Asp/His) box polypeptide RIG1
Probable ATP dependent RNA helicase DDX58
Probable ATP-dependent RNA helicase DDX58
Retinoic acid inducible gene 1 protein
Retinoic acid-inducible gene 1 protein
Retinoic acid-inducible gene I protein
RNA helicase RIG I
FunctionInvolved in innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, triggers a transduction cascade involving MAVS/IPS1, which results in the activation of NF-kappa-B, IRF3 and IRF7 and the induction of the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). Essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza viruses, Japanese encephalitis virus and HCV.
Tissue specificityPresent in vascular smooth cells (at protein level).
Sequence similaritiesBelongs to the helicase family. Contains 2 CARD domains. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
DomainThe repressor domain controls homomultimerization and interaction with MAVS. The helicase domain is responsible for dsRNA recognition. The 2 CARD domains are responsible for interaction with and signaling through MAVS. The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.
Post-translational modificationsIsgylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. Ubiquitinated. Undergoes 'Lys-63'-linked ubiquitination. Lys-172 is the critical site for TRIM25-mediated ubiquitination, for MAVS binding and to induce anti-viral signal transduction. Lys-154, Lys-164 and Lys-172 are critical sites for RNF135-mediated ubiquitination. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains.
Cellular localizationCytoplasm. Colocalized with TRIM25 at cytoplasmic perinuclear bodies.