06-1040
Anti-RIG-I (NT) Antibody
from rabbit, purified by affinity chromatography
Synonym(s):
Probable ATP-dependent RNA helicase DDX58, DEAD box protein 58, Retinoic acid-inducible gene 1 protein, RIG-1, Retinoic acid-inducible gene I protein, RIG-I
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
biological source
rabbit
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
Quality Level
General description
Retinoic acid-inducible gene 1 protein (RIG-1) is a cytoplasmic DExD/H box RNA helicase belonging to the helicase family and containing 2 CARD domains within the N-terminus, a repressor domain (RD), a helicase ATP-binding domain and a helicase C-terminal binding domain. RIG-1 is able to bind the 5’-triphosphate RNA of single or double-stranded viral RNA. After recognizing and binding viral RNA, RIG-1 protein initializes type I IFN production, and within fibroblasts and dendritic cells plays a central role in the regulation of type I IFN production in response to viral presence. There are four known isoforms resulting from alternative splice variants.
~102 kDa observed
Immunogen
Epitope: N-terminus
GST-tagged recombinant protein corresponding to the N-terminus of human RIG-I.
Application
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in IP. (Paz, S., et al. (2011). Cell Research. 1-16.)
Research Category
Inflammation & Immunology
Inflammation & Immunology
Research Sub Category
Immunoglobulins & Immunology
Immunoglobulins & Immunology
Use Anti-RIG-I (N-Terminus) Antibody (Rabbit Polyclonal Antibody) validated in WB, IP to detect RIG-I (N-Terminus) also known as Retinoic acid-inducible gene 1 protein.
Biochem/physiol Actions
Other homologies: Rhesus Monkey (99% sequence homology).
This antibody recognizes RIG-I at the N-terminus.
Physical form
Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
SeV treated and untreated A549 cell lysates
SeV treated and untreated A549 cell lysates
Evaluated by Western Blot in SeV treated and untreated A549 cell lysates.
Western Blot Analysis: 0.05 µg/mL of this antibody detected RIG-I on 10 µg of SeV untreated and treated A549 cell lysates.
Western Blot Analysis: 0.05 µg/mL of this antibody detected RIG-I on 10 µg of SeV untreated and treated A549 cell lysates.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response.
Paz, S; Vilasco, M; Werden, SJ; Arguello, M; Joseph-Pillai, D; Zhao, T; Nguyen, TL; Sun et al.
Cell research null
Silvia Albertini et al.
Journal of immunology (Baltimore, Md. : 1950), 200(6), 2076-2089 (2018-02-02)
Although it is clear that high-risk human papillomaviruses (HPVs) can selectively infect keratinocytes and persist in the host, it still remains to be unequivocally determined whether they can escape antiviral innate immunity by interfering with pattern recognition receptor (PRR) signaling.
Irene Lo Cigno et al.
Journal of virology, 94(4) (2019-11-30)
Subversion of innate immunity by oncoviruses, such as human papillomavirus (HPV), favors carcinogenesis because the mechanism(s) of viral immune evasion can also hamper cancer immunosurveillance. Previously, we demonstrated that high-risk (hr) HPVs trigger simultaneous epigenetic silencing of multiple effectors of
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