Mouse Anti-TICAM1 Recombinant Antibody (CBYJT-3120) (CBMAB-T2388-YJ)

Mouse

Human

CBYJT-3120

IgG

WB, IP, IF, ELISA

Human

IgG

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

PBS, pH 7.4

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Toll Like Receptor Adaptor Molecule 1

TICAM1 is an adaptor protein containing a Toll/interleukin-1 receptor (TIR) homology domain, which is an intracellular signaling domain that mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TICAM1 is involved in native immunity against invading pathogens. TICAM1 specifically interacts with toll-like receptor 3, but not with other TLRs, and this association mediates dsRNA induction of interferon-beta through activation of nuclear factor kappa-B, during an antiviral immune response.

Toll Like Receptor Adaptor Molecule 1; Toll-Interleukin-1 Receptor Domain-Containing Adapter Protein Inducing Interferon Beta; Proline-Rich, Vinculin And TIR Domain-Containing Protein B; TIR Domain-Containing Adapter Protein Inducing IFN-Beta; Putative NF-Kappa-B-Activating Protein 502H; TIR Domain-Containing Adapter Molecule 1; MyD88-3

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).
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).

Biological Process apoptotic signaling pathwaySource:Ensembl
Biological Process B cell proliferationSource:Ensembl
Biological Process cellular response to lipopolysaccharideSource:ParkinsonsUK-UCL
Biological Process cellular response to oxidised low-density lipoprotein particle stimulusSource:ARUK-UCL
Biological Process defense response to virusSource:UniProtKB-KW
Biological Process I-kappaB kinase/NF-kappaB signalingSource:Ensembl
Biological Process inflammatory responseSource:UniProtKB-KW
Biological Process innate immune responseSource:UniProtKB-KW
Biological Process lipopolysaccharide-mediated signaling pathwaySource:GO_Central1 Publication
Biological Process macrophage activation involved in immune responseSource:Ensembl
Biological Process nitric oxide biosynthetic processSource:Ensembl
Biological Process positive regulation of autophagySource:ParkinsonsUK-UCL
Biological Process positive regulation of B cell proliferationSource:Ensembl
Biological Process positive regulation of chemokine productionSource:Ensembl
Biological Process positive regulation of cytokine production involved in inflammatory responseSource:ARUK-UCL
Biological Process positive regulation of gene expressionSource:ARUK-UCL
Biological Process positive regulation of I-kappaB kinase/NF-kappaB signalingSource:UniProtKB1 Publication
Biological Process positive regulation of interferon-beta productionSource:Ensembl
Biological Process positive regulation of interleukin-6 productionSource:Ensembl
Biological Process positive regulation of macrophage cytokine productionSource:Ensembl
Biological Process positive regulation of myeloid dendritic cell cytokine productionSource:UniProtKB
Biological Process positive regulation of natural killer cell activationSource:GO_Central1 Publication
Biological Process positive regulation of NF-kappaB transcription factor activitySource:GO_Central1 Publication
Biological Process positive regulation of nitric oxide biosynthetic processSource:Ensembl
Biological Process positive regulation of protein bindingSource:Ensembl
Biological Process positive regulation of protein ubiquitinationSource:Ensembl
Biological Process positive regulation of tumor necrosis factor productionSource:Ensembl
Biological Process regulation of protein-containing complex assemblySource:Ensembl
Biological Process response to exogenous dsRNASource:MGI1 Publication
Biological Process TRIF-dependent toll-like receptor signaling pathwaySource:CACAO1 Publication

Cytoplasmic vesicle, autophagosome
Cytoplasm, cytosol
Mitochondrion
Colocalizes with UBQLN1 in the autophagosome (PubMed:21695056).
Colocalizes in the cytosol with DDX1, DDX21 and DHX36. Colocalizes in the mitochondria with DDX1 and poly(I:C) RNA ligand. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (By similarity).

Encephalopathy, acute, infection-induced, 6, herpes-specific (IIAE6):
A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. It is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.

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.1 Publication
(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.