Recombinant Human TRIF protein (GST tag N-Terminus)
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Recombinant Human TRIF protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 110 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
PRVTIRB, TRIF, TICAM1, TIR domain-containing adapter molecule 1, TICAM-1, Putative NF-kappa-B-activating protein 502H, Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta, MyD88-3, TIR domain-containing adapter protein inducing IFN-beta
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TRIF protein (GST tag N-Terminus) (AB153605)
ab153605 on a 12.5% SDS-PAGE 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
TRIF is part of the innate immune response mechanism. It functions as a central component in signal transduction processes especially in response to pathogen-associated molecular patterns (PAMPs). TRIF often forms complexes with other signaling proteins to activate transcription factors such as IRF3 and NF-kB which stimulate the expression of inflammatory cytokines and antiviral genes. This function allows the body to respond quickly to infections and initiate immune defenses.
Pathways
TRIF participates in important immune signaling pathways notably the TLR and interferon signaling pathways. In the TLR pathway TRIF interacts with proteins such as MyD88 and TRAF6 to propagate signals from TLR4 critical in detecting Gram-negative bacteria. Through its role in the interferon signaling pathway TRIF helps in the regulation of antiviral responses and is essential for the expression of interferon-stimulated genes that combat viral infections.
Specifications
Form
Liquid
General info
Function
Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis (PubMed : 12471095, PubMed : 12539043, PubMed : 14739303, PubMed : 28747347, PubMed : 35215908). Ligand binding to these receptors results in TRIF recruitment through its TIR domain (PubMed : 12471095, PubMed : 12539043, PubMed : 14739303). Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively (PubMed : 12471095, PubMed : 12539043, PubMed : 14739303). Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens (PubMed : 25636800). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines (By similarity).
Post-translational modifications
Phosphorylated by TBK1 (PubMed:14530355, PubMed:25636800). Following activation, phosphorylated by TBK1 at Ser-210 in the pLxIS motif (PubMed:25636800). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (PubMed:25636800, PubMed:27302953).. Polyubiquitinated at Lys-229 by TRIM38 with 'Lys-48'-linked chains, leading to proteasomal degradation (PubMed:23056470). Polyubiquitinated with 'Lys-6'- and 'Lys-33'-linked chains in a TRIM8-dependent manner; ubiquitination disrupts the interaction with TBK1 and subsequent interferon production (PubMed:28747347).. (Microbial infection) Cleaved and degraded by hepatitis A virus (HAV) protein 3CD allowing the virus to disrupt host TLR3 signaling.. (Microbial infection) Cleaved by CVB3 protease 3C allowing the virus to disrupt host TLR3 signaling.. (Microbial infection) Cleaved by Seneca Valley virus protease 3C allowing the virus to disrupt host TLR3 signaling.. (Microbial infection) Cleaved by protease 3C of human enterovirus D68 (EV68) allowing the virus to disrupt host TLR3 signaling.. (Microbial infection) Cleaved by HCV protease NS3/4A, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state.
Subcellular localisation
Mitochondrion
Target data
Product promise
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