Recombinant Human RIG-I/DDX58 Protein

Name: Recombinant Human RIG-I/DDX58 Protein
Brand: Beta LifeScience
SKU: BLA-7805P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	O95786
Synonym	Ddx58 DDX58_HUMAN 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 DKFZp434J1111 DKFZp686N19181 FLJ13599 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 RIG I Rig-1 RIG-I RIG1 rigi RLR 1 RNA helicase RNA helicase RIG I SGMRT2
Description	Recombinant Human RIG-I/DDX58 Protein was expressed in Wheat germ. It is a Full length protein
Source	Wheat germ
AA Sequence	MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGP MEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKL EEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMA GAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDL EDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLEL ALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQI PVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQI LVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSG PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELE QVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQ NREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYND ALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESV SRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGN PKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVA DEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEK EQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPV PDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKP KQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATG VQTLYSKWKDFHFEKIPFDPAEMSK
Molecular Weight	133 kDa including tags
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and proinflammatory cytokines. Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments. The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms. Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons. Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotaviruses and reoviruses. Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.63). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.
Subcellular Location	Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cell junction, tight junction. Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.
Protein Families	Helicase family, RLR subfamily
Database References	HGNC: 19102 OMIM: 609631 KEGG: hsa:23586 STRING: 9606.ENSP00000369213 UniGene: Hs.190622
Associated Diseases	Singleton-Merten syndrome 2 (SGMRT2)
Tissue Specificity	Present in vascular smooth cells (at protein level).

Gene Functions References

These results refine the RNA sensing paradigm for nuclear-replicating viruses and reveal a previously unrecognized subcellular milieu for RIG-I-like receptor sensing. PMID: 30097581
fascin1 constitutively interacts with IkappaB kinase (IKK) in the RIG-I signaling pathway. In summary, we have identified fascin1 as a suppressor of the RIG-I signaling pathway associating with IkappaB kinase in DLD-1 colon cancer cells to suppress immune responses to viral infection. PMID: 29496994
The structure of RIG-I C268F in complex with double-stranded RNA reveals that C268F helps induce a structural conformation in RIG-I that is similar to that induced by ATP PMID: 30047865
FBXW7 is critical for RIG-I stabilization during antiviral responses. PMID: 28287082
These findings imply a novel function for DDX6 as an RNA co-sensor and signaling enhancer for RIG-I. PMID: 29949917
Identification of a second binding site on the RIG-I TRIM25 B30.2 domain has been reported. PMID: 29259080
Aging thus compromises both the primary and secondary RIG-I signaling pathways that govern expression of type I IFN genes, thereby impairing antiviral resistance to IAV. PMID: 29233916
RIG-I-like receptors have a role in induction of interferon-beta1 in antiviral gene expression PMID: 29098213
MCCC1 plays an essential role in virus-triggered, MAVS-mediated activation of NF-kappaB signaling. PMID: 27629939
The authors find that KHSRP associates with the regulatory domain of RIG-I to maintain the receptor in an inactive state and attenuate its sensing of viral RNA (vRNA). PMID: 28248290
In this study, the authors determined that, in contrast to the RIG-I CARD domain, full-length RIG-I must undergo K63-linked ubiquitination at multiple sites to reach full activity. PMID: 27387525
RIG-1 overexpression is protective for cigarette smoke exposure enhanced susceptibility to influenza infection. PMID: 28865477
These results showed that the knockdown of RIGI reduced the inhibition of cell proliferation, cell cycle arrest and apoptosis in the alltrans retinoic acid induced NB4 acute promyelocytic leukemia cells via the AKTFOXO3A signaling pathway. PMID: 28656276
The host RIG-I signaling pathway is a key early obstacle to paramyxovirus infection, as it results in rapid induction of an antiviral response. This study shows that paramyxovirus V proteins interact with and inhibit the activation of RIG-I, thereby interrupting the antiviral signaling pathway and facilitating virus replication. PMID: 29321315
These findings indicated that hepatitis B virus-induced miR146a attenuates cell-intrinsic anti-viral innate immunity through targeting RIG-I and RIG-G. PMID: 27210312
Taken together, these findings reveal an essential role of CypA in boosting RIG-I-mediated antiviral immune responses by controlling the ubiquitination of RIG-I and MAVS. PMID: 28594325
RIG-I-like receptors (RLRs) are well-known viral RNA sensors in the cytoplasm that recognize the nonself signatures of viral RNAs to trigger IFN responses. PMID: 28475461
Knockdown of PBRM1 in colon cancer cells increased the expression of two receptor genes (RIG-I and MDA5) and upregulated interferon (IFN)-related and inflammation-related gene signatures. PMID: 28940253
Dengue virus infection of human dendritic cells drives follicular T helper cells formation via crosstalk of RIG-I and MDA5. PMID: 29186193
DDX58_rs10813831 T-allele may be associated with a reduced risk of nodular sclerosis EBV-related cHL, which suggests a role for RIG-I (retinoic acid-inducible gene I), encoded by DDX58, in these cases. PMID: 27267403
mutations in the genes encoding for RIG-I and MDA5 have been identified to cause rare diseases including Aicardi-Goutieres syndrome, Systemic Lupus Erythematosus in certain individuals as well as classic and atypical Singleton-Merten syndrome. Patients carrying mono-allelic mutations in MDA5 and RIG-I show constitutive activation of the RIG-I receptors and downstream signalling PMID: 26993858
These findings demonstrate how IFNgamma induced CK2 regulates RIG-I to drive a complex program of metabolic adaptation and redox homeostasis, crucial for determining glioma cell fate. PMID: 26631910
Data show that host-derived RNAs, most prominently 5S ribosomal RNA pseudogene 141 (RNA5SP141), bound to RIG-I during infection with herpes simplex virus 1 (HSV-1). PMID: 29180807
RIG-I expression is markedly increased in the affected skin derived from psoriasis patients and from both IL-23- and imiquimod -induced psoriasis-like mouse model. PMID: 28377495
DDX58 was confirmed to be the downstream target of TRIM24, whose downregulation is essential for the migratory phenotype induced by GLUT4-TRIM24 activation in head and neck squamous cell carcinoma cells. PMID: 28061796
TRIM25 actively participates in higher-order assembly of the RIG-I signalosome. PMID: 27425606
This study evaluation the roles of SOCS1, the regulator of TLR9, RIG-I, and CD152 in patients with liver fibrosis/cirrhosis; the use of polymorphisms as markers for genetic risk is reported. PMID: 28762092
study documents that recombinant measles virus produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I and LGP2 proteins, both of which are cytosolic nonself RNA sensors of innate immunity. PMID: 28768856
findings define the WHIP-TRIM14-PPP6C mitochondrial signalosome required for RIG-I-mediated innate antiviral immunity. PMID: 29053956
both IL-6 and RIG-I are downstream molecules of STING along the DNA sensor pathway. PMID: 28806404
These data suggest that prior exposure to IFN-gamma may leave an epigenetic mark on the chromatin that enhances airway cells' ability to resist infection, possibly via epigenetic upregulation of RIG-I. PMID: 28481620
findings show that RIG-I and MDA5 triggering by dengue virus leads to TH1 polarization, which is characterized by high levels of IFN-gamma; identified RIG-I and MDA5 as critical players in innate and adaptive immune responses against Dengue virus PMID: 28507028
Results identified a negative-feedback mechanism that targets RIG-I activity mediated by DAPK1. RIG-I-mediated antiviral signaling activates DAPK1 kinase activity and DAPK1 inactivates RIG-I RNA sensing by direct phosphorylation of RIG-I. PMID: 28132841
Mechanistically, West Nile virus NS1 targets RIG-I and melanoma differentiation-associated gene 5 (MDA5) by interacting with them and subsequently causing their degradation by the proteasome. PMID: 28659477
RIG-I stimulates the cellular innate immunity against hepatitis E virus infections. PMID: 28195391
dynamic sumoylation and desumoylation of MDA5 and RIG-I modulate efficient innate immunity to RNA virus and its timely termination. PMID: 28250012
Taken together, the present study reveals that T80 phosphorylation of influenza A virus NS1 reduced virus replication through controlling RIG-I-mediated interferon production and viral ribonucleoprotein activity. PMID: 27376632
results suggest that RNAs containing modified nucleotides interrupt signaling at early steps of the RIG-I-like innate immune activation pathway PMID: 27651356
The authors found that in Sendai virus C protein deletion mutant-infected cells, Sendai virus defective interfering RNA also functioned as an exclusive RIG-I ligand. PMID: 28631605
ArfGAP domain-containing protein 2 (ADAP2) is identified as a key novel scaffolding protein that integrates different modules of the RIG-I pathway, located at distinct subcellular locations, and mediates cellular antiviral type I interferon production. PMID: 27956705
the bending structure of the panhandle RNA negates the requirement of a 5'-PPP moiety for RIG-I activation. PMID: 27288441
RIG-I-like receptor-induced IRF3 mediated pathway of apoptosis (RIPA): a new antiviral pathway PMID: 27815826
The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. PMID: 28148787
The regulation of STING via RIG-I-mediated innate immune sensing. PMID: 27512060
These results suggest that inhibition of RIG-I-mediated type I interferon responses by Enterovirus 71 may contribute to the pathogenesis of viral infection. PMID: 27633794
Modulates RIG-I-dependent antiviral response is through post-translational modifications of or protein-protein interactions with RIG-I. [review] PMID: 27572506
Pyruvate carboxylase activates the RIG-I-like receptor-mediated antiviral immune response by targeting the MAVS signalosome. PMID: 26906558
This study shows that RIG-I activation results in MKP-1-mediated inhibition of cell proliferation in melanoma cells via controlling the p38-HSP27, c-Jun and rpS6 pathways PMID: 26829212
HepaRG cells express a similar pattern of functional TLR/RLR as compared to PHH, thus qualifying HepaRG cells as a surrogate model to study pathogen interactions within a hepatocyte innate system. PMID: 26144659
COPD patients had higher interleukin (IL)-1 and IL-8 mRNA expression levels, and these inflammatory cytokines positively correlate with MDA-5 levels. However, there was no difference in the expression of RIG-I between COPD patients and control subjects. PMID: 24992168

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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