Recombinant Human MDA5 protein
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Recombinant Human MDA5 protein is a Human Fragment protein, in the 928 to 1023 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
MDA5, RH116, IFIH1, Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, Helicase with 2 CARD domains, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, Murabutide down-regulated protein, RIG-I-like receptor 2, RNA helicase-DEAD box protein 116, CADM-140 autoantigen, Helicard, MDA-5, RLR-2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human MDA5 protein (AB112423)
ab112423 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
In cellular defense mechanisms MDA5 plays an important role in initiating antiviral responses. It operates as part of a signaling complex that includes MAVS (mitochondrial antiviral-signaling protein) leading to the production of type I interferons and pro-inflammatory cytokines. These responses promote an antiviral state in host cells aiding in the containment and clearance of viral infections. MDA5 antibodies can be useful tools for studying these immune processes.
Pathways
MDA5 interacts with antiviral signaling pathways such as the IFN signaling pathway and the RIG-I-like receptor signaling pathway. Upon recognizing viral RNA MDA-5 cooperates with proteins like RIG-I and MAVS to activate downstream signaling cascades that mediate immune responses. This collaboration enables efficient viral recognition and response limiting viral replication and spread.
Specifications
Form
Liquid
General info
Function
Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and pro-inflammatory cytokines (PubMed : 28594402, PubMed : 32169843, PubMed : 33727702). Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length) (PubMed : 22160685). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases : TBK1 and IKBKE which phosphorylate interferon regulatory factors : IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and rhinovirus (PubMed : 28606988). Detects coronavirus SARS-CoV-2 (PubMed : 33440148, PubMed : 33514628). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines.
Sequence similarities
Belongs to the helicase family. RLR subfamily.
Post-translational modifications
Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta.. Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). USP17/UPS17L2-dependent deubiquitination positively regulates the receptor (PubMed:20368735). Ubiquitinated by TRIM25 via 'Lys-63'-linked ubiquitination, promoting activation of IFIH1/MDA5 (PubMed:30193849). Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation (PubMed:29117565). Ubiquitinated by TRIM65 via 'Lys-63'-linked ubiquitination, promoting activation of IFIH1/MDA5 (PubMed:28594402).. ISGylated by ISG15. ISGylation increases upon infection with dengue (DENV) or Zika (ZIKV) viruses. ISGylation at Lys-23 and Lys-43 is dependent of dephosphorylation at Ser-88, regulates mitochondrial translocation and oligomerization. Essential for IFIH1/MDA5-mediated cytokine responses and restriction of virus replication.. Phosphorylated at Ser-88 (PubMed:23499489, PubMed:33727702). Dephosphorylated by phosphatases PPP11CA/PPP11CC; dephosphorylation precedes and is required for ISGylation (PubMed:23499489, PubMed:33727702).. During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation.. (Microbial infection) Cleaved and inactivated by the protease 2A of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production.
Subcellular localisation
Nucleus
Target data
Product promise
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