Datasheet

生物学的記述

Specificity	MAVS Antibody [H8N11] detects endogenous levels of total MAVS protein.
Background	MAVS (mitochondrial antiviral‑signaling protein; also VISA/IPS‑1/Cardif) is a CARD‑containing adaptor anchored in the outer mitochondrial membrane and related organellar membranes, where it functions as the central signaling hub for RIG‑I‑like receptor detection of viral RNA, converting transient cytosolic sensor engagement into prion‑like signaling assemblies that drive IRF and NF‑κB activation and type I interferon production. The protein architecture combines an N‑terminal CARD that mediates homotypic interactions with the CARDs of RIG‑I and MDA5, a proline‑rich central segment that recruits TRAF E3 ligases and other scaffolds, and a C‑terminal transmembrane helix that anchors MAVS to mitochondria, peroxisomes, and mitochondria‑associated ER membranes, placing the signaling platform at strategically positioned intracellular sites. Upon sensing viral RNA, RIG‑I/MDA5 undergo K63‑linked ubiquitination and oligomerization and engages the MAVS CARD, triggering a conformational transition in MAVS into higher‑order, filamentous aggregates with prion‑like properties that self‑propagate along the mitochondrial network and nucleate large signaling complexes containing TRAF2/3/5/6, TANK, TBK1, and the IKKα/β/γ complex. These assemblies drive phosphorylation of IRF3/IRF7 and IκB, leading to nuclear translocation of IRF and NF‑κB transcription factors and the coordinated induction of type I and III interferons, pro‑inflammatory cytokines, and antiviral effector genes, and MAVS‑dependent pathways also intersect with apoptotic machinery via caspase‑8 to eliminate infected cells. Genetic ablation of MAVS in mice abolishes RIG‑I/MDA5‑mediated IFN induction and IRF3/NF‑κB activation in most cell types, renders animals unable to mount effective innate responses to RNA viruses, and results in high viral loads and lethality after poly(I:C) challenge or infection with multiple RNA viruses, while leaving TLR‑ and cytosolic DNA–dependent IFN pathways largely intact, demonstrating that MAVS is specifically essential for the RLR arm of antiviral immunity. Post‑translational control of MAVS, particularly ubiquitylation, provides additional layers of signal tuning: K63‑linked ubiquitination by several E3 ligases (including TRIM31 and MARCH5) promotes MAVS aggregation and signaling competence, whereas K48‑linked ubiquitination by ligases such as RNF125 targets MAVS for proteasomal degradation and terminates signaling, and a growing set of deubiquitylating enzymes removes these chains to reset the pathway, collectively making the ubiquitylation status of MAVS a critical determinant of amplitude and duration of the antiviral response. Multiple RNA and DNA viruses—including HCV, picornaviruses, and herpesviruses—encode proteases or mitochondrial modulators that cleave or displace MAVS from membranes, disrupt its aggregation, or manipulate its ubiquitylation, underlining the adaptor’s central position at the host–virus interface and highlighting MAVS as both a vulnerability targeted by pathogens and a potential therapeutic node for modulating innate immunity and inflammatory pathology beyond classic viral infection, such as in sepsis and sterile tissue injury.

Specificity

MAVS Antibody [H8N11] detects endogenous levels of total MAVS protein.

Background

MAVS (mitochondrial antiviral‑signaling protein; also VISA/IPS‑1/Cardif) is a CARD‑containing adaptor anchored in the outer mitochondrial membrane and related organellar membranes, where it functions as the central signaling hub for RIG‑I‑like receptor detection of viral RNA, converting transient cytosolic sensor engagement into prion‑like signaling assemblies that drive IRF and NF‑κB activation and type I interferon production. The protein architecture combines an N‑terminal CARD that mediates homotypic interactions with the CARDs of RIG‑I and MDA5, a proline‑rich central segment that recruits TRAF E3 ligases and other scaffolds, and a C‑terminal transmembrane helix that anchors MAVS to mitochondria, peroxisomes, and mitochondria‑associated ER membranes, placing the signaling platform at strategically positioned intracellular sites. Upon sensing viral RNA, RIG‑I/MDA5 undergo K63‑linked ubiquitination and oligomerization and engages the MAVS CARD, triggering a conformational transition in MAVS into higher‑order, filamentous aggregates with prion‑like properties that self‑propagate along the mitochondrial network and nucleate large signaling complexes containing TRAF2/3/5/6, TANK, TBK1, and the IKKα/β/γ complex. These assemblies drive phosphorylation of IRF3/IRF7 and IκB, leading to nuclear translocation of IRF and NF‑κB transcription factors and the coordinated induction of type I and III interferons, pro‑inflammatory cytokines, and antiviral effector genes, and MAVS‑dependent pathways also intersect with apoptotic machinery via caspase‑8 to eliminate infected cells. Genetic ablation of MAVS in mice abolishes RIG‑I/MDA5‑mediated IFN induction and IRF3/NF‑κB activation in most cell types, renders animals unable to mount effective innate responses to RNA viruses, and results in high viral loads and lethality after poly(I:C) challenge or infection with multiple RNA viruses, while leaving TLR‑ and cytosolic DNA–dependent IFN pathways largely intact, demonstrating that MAVS is specifically essential for the RLR arm of antiviral immunity. Post‑translational control of MAVS, particularly ubiquitylation, provides additional layers of signal tuning: K63‑linked ubiquitination by several E3 ligases (including TRIM31 and MARCH5) promotes MAVS aggregation and signaling competence, whereas K48‑linked ubiquitination by ligases such as RNF125 targets MAVS for proteasomal degradation and terminates signaling, and a growing set of deubiquitylating enzymes removes these chains to reset the pathway, collectively making the ubiquitylation status of MAVS a critical determinant of amplitude and duration of the antiviral response. Multiple RNA and DNA viruses—including HCV, picornaviruses, and herpesviruses—encode proteases or mitochondrial modulators that cleave or displace MAVS from membranes, disrupt its aggregation, or manipulate its ubiquitylation, underlining the adaptor’s central position at the host–virus interface and highlighting MAVS as both a vulnerability targeted by pathogens and a potential therapeutic node for modulating innate immunity and inflammatory pathology beyond classic viral infection, such as in sepsis and sterile tissue injury.

使用情報

Application

WB, IP, IF, FCM

Dilution

WB	IP	IF	FCM
1:1000	1:50	1:100 - 1:400	1:200 - 1:800

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

56 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/34566944/
https://pubmed.ncbi.nlm.nih.gov/16713980/

MAVS Antibody [H8N11]

生物学的記述

使用情報

References

Application Data