Analytical Data
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Gene name
RIGI
- Application
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Alternative Names
RIGI；DDX58；Antiviral innate immune response receptor RIG-I
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95786
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Expression Region
1-430aa
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AA Sequence
MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKL
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Molecular Weight
53.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
RIG-I (retinoic acid-inducible gene I) is a crucial cytosolic pattern recognition receptor that plays a significant role in the innate immune response against viral infections. It specifically recognizes 5' triphosphate (3pRNA) and short double-stranded RNA molecules, triggering the activation of downstream signaling pathways that lead to the production of type I interferons and pro-inflammatory cytokines. Research on RIG-I is driven by its potential as a target for therapeutic interventions in viral diseases, including influenza and RNA viruses like Ebola and Zika. The interest in RIG-I has intensified with the increasing threat of emerging viral outbreaks and the need for novel antiviral strategies. Additionally, understanding RIG-I’s structural and functional mechanisms can aid in developing biomimetic therapies and enhancing vaccine efficacy. Recent advances in recombinant protein technology have enabled researchers to produce RIG-I proteins for functional assays, structural studies, and high-throughput screening of small molecules that modulate its activity. These studies pave the way for a deeper understanding of RIG-I's regulatory roles in immune signaling and its potential application in immunotherapy and vaccine development, reflecting the broader goal of enhancing host defense mechanisms against pathogenic infections.
