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AdipoGen Life Sciences
anti-RIG-I, mAb (Alme-1)
495
CHF
CHF 495.00
In stock
AG-20B-0009-C100100 µgCHF 495.00
Figure 1: Immunohistochemical staining of endogenous human RIG-I in different human tissues (paraffin sections) using anti-RIG-I, mAb (Alme-1) (Prod. No. AG-20B-0009).
Different human normal tissues (A: Nasopharynx; B: Colon; C: Endometrium) or cancer tissues (D: Breast; E: Skin; F: Ovarian) were stained with anti-RIG-I, mAb (Alme-1) by standard immunohistochemistry.
Different human normal tissues (A: Nasopharynx; B: Colon; C: Endometrium) or cancer tissues (D: Breast; E: Skin; F: Ovarian) were stained with anti-RIG-I, mAb (Alme-1) by standard immunohistochemistry.
Figure 2: Western blot analysis of human RIG-I in HeLa cells by using RIG-I, mAb (Alme-1) (Prod. No. AG-20B-0009).
Method: Cell extracts from HeLa cells either unstimulated (lane 1) or stimulated for 6h (lane 2), 16h (lane 3) or 24 h (lane 4) with Interferon γ were resolved by SDS-PAGE under reducing conditions, transferred to nitrocellulose and incubated with the RIG-I , mAb (Alme-1) at a 1:1000 dilution for 1 hour. Proteins were visualized using a peroxidase-conjugated polyclonal antibody to mouse IgG and a chemiluminescence detection system.
Method: Cell extracts from HeLa cells either unstimulated (lane 1) or stimulated for 6h (lane 2), 16h (lane 3) or 24 h (lane 4) with Interferon γ were resolved by SDS-PAGE under reducing conditions, transferred to nitrocellulose and incubated with the RIG-I , mAb (Alme-1) at a 1:1000 dilution for 1 hour. Proteins were visualized using a peroxidase-conjugated polyclonal antibody to mouse IgG and a chemiluminescence detection system.
| Product Details | |
|---|---|
| Synonyms | RIG-1; Retinoic Acid-inducible Gene 1 Protein; DEAD-box Protein 58; Probable ATP-dependent RNA Helicase DDX58 |
| Product Type | Monoclonal Antibody |
| Properties | |
| Clone | Alme-1 |
| Isotype | Mouse IgG1 |
| Source/Host | Purified from concentrated hybridoma tissue culture supernatant. |
| Immunogen/Antigen | Recombinant human RIG-I (aa 201-713). |
| Application |
Immunohistochemistry: (paraffin sections) |
| Crossreactivity |
Human Mouse |
| Specificity |
Recognizes human and mouse RIG-I. |
| Purity | ≥95% (SDS-PAGE) |
| Purity Detail | Protein G-affinity purified. |
| Concentration | 1mg/ml |
| Formulation | Liquid. In PBS containing 10% glycerol and 0.02% sodium azide. |
| Isotype Negative Control | |
| Shipping and Handling | |
| Shipping | BLUE ICE |
| Short Term Storage | +4°C |
| Long Term Storage | -20°C |
| Handling Advice |
After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. |
| Use/Stability | Stable for at least 1 year after receipt when stored at -20°C. |
| Documents | |
| MSDS |
 Download PDF |
| Product Specification Sheet | |
| Datasheet |
Download PDF |
Description
RIG-I and MDA5 are highly conserved helicases involved in the innate immune response to virus. RIG-I is a member of the DEAD-box RNA helicases and is activated by cytoplasmic dsRNA and 5’-ppp RNA produced during the viral replication. The protein is characterized by a N-terminal region with two caspase recruitment domains (CARD) and a C-terminal region harboring potential ATP-dependent RNA helicase activity. RIG-I recruits the CARD adaptor inducing IFN-β (Cardif) in a CARD-CARD-dependent manner resulting in NF-κB and IRF3 activation.
Product References
- The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases: M. Rebsamen, et al.; Cell Death Differ. 15, 1804 (2008)
- Phosphorylation-mediated negative regulation of RIG-I antiviral activity: M.U. Gack, et al.; J. Virol. 84, 3220 (2010)
- Incoming RNA Virus Nucleocapsids Containing a 5'-Triphosphorylated Genome Activate RIG-I and Antiviral Signaling: M. Weber, et al.; Cell Host Microbe 13, 336 (2013)
- Lymphocytic choriomeningitis virus differentially affects the virus-induced type I interferon response and mitochondrial apoptosis mediated by RIG-I/MAVS: C. Pythoud, et al.; J. Virol. 89, 6240 (2015)
- A phosphomimetic-based mechanism of dengue virus to antagonize innate immunity: Y.K. Chan & M.U. Gack; Nat. Immunol. 17, 523 (2016)
- Sensing of latent EBV infection through exosomal transfer of 5'pppRNA: S.R. Baglio, et al.; PNAS 113, E587 (2016)
- RNAs Containing Modified Nucleotides Fail To Trigger RIG-I Conformational Changes for Innate Immune Signaling: A. Fiegen Durbin, et al.; MBio 7, e00833 (2016)
- Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity: J.J. Chiang, et al.; Nat. Immunol. 19, 53 (2018)
- RIG-I recognizes the 5′ region of dengue and zika virus genomes: M. Chazal, et al.; Cell Rep. 24, 320 (2018)
- The Human Papillomavirus E6 Oncoprotein Targets USP15 and TRIM25 To Suppress RIG-I-Mediated Innate Immune Signaling: C. Chiang, et al.; J. Virol. 92, e01737-17 (2018) [KO Validation]
- Zika virus NS3 mimics a cellular 14-3-3-binding motif to antagonize RIG-I- and MDA5-mediated innate immunity: W. Riedl, et al.; Cell Host Microbe 26, 493 (2019)
- Influenza A virus M2 protein triggers mitochondrial DNA-mediated antiviral immune responses: M. Moriyama, et al.; Nat. Comm. 10, 6424 (2019)
- Attenuation of the Innate Immune Response against Viral Infection Due to ZNF598-Promoted Binding of FAT10 to RIG-I: G. Wang, et al.; Cell Rep. 28, 1961 (2019)
- ISG15-dependent activation of the sensor MDA5 is antagonized by the SARS-CoV-2 papain-like protease to evade host innate immunity: GQ. Liu, et al.; Nat. Microbiol. 6, 465 (2021)
- NSs of the mildly virulent sandfly fever Sicilian virus is unable to inhibit interferon signaling and upregulation of interferon-stimulated genes: J.D. Wuerth & F. Weber; J. Gen. Virol. 102, (2021)
- Viral Protein Accumulation of Zika Virus Variants Links with Regulation of Innate Immunity for Differential Control of Viral Replication, Spread, and Response to Interferon: A.Y. Lu, et al.; J. Virol. 97, e0198222 (2023)
- Acetylation of the NS3 helicase by KAT5g is essential for flavivirus replication: T. Serman, et al.; Cell Host Microbe 31, 1317 (2023)
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