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anti-Human TICAM2 Antibodies:
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Human Polyclonal TICAM2 Primary Antibody for IHC (fro), WB - ABIN550261
ONeill, Fitzgerald, Bowie: The Toll-IL-1 receptor adaptor family grows to five members. in Trends in immunology 2003
Show all 2 Pubmed References
Human Polyclonal TICAM2 Primary Antibody for WB - ABIN1169199
Aksoy, Albarani, Nguyen, Laes, Ruelle, De Wit, Willems, Goldman, Goriely: Interferon regulatory factor 3-dependent responses to lipopolysaccharide are selectively blunted in cord blood cells. in Blood 2007
Human Polyclonal TICAM2 Primary Antibody for DB, ELISA - ABIN2747722
Keck, Müller, Fejer, Savic, Tchaptchet, Nielsen, Galanos, Huber, Freudenberg: Absence of TRIF signaling in lipopolysaccharide-stimulated murine mast cells. in Journal of immunology (Baltimore, Md. : 1950) 2011
SLAMF1 is required for TLR4-mediated TRAM-TRIF-dependent signaling in human macrophages.
Data suggest that endosomal localization of TICAM2 is essential for TLR4-mediated type I interferon-inducing signaling from endosomes; TICAM2 acts as scaffold protein and activates TICAM1; N-terminal myristoylation allows TICAM2 to anchor to endosomal membrane. (TICAM2 = toll like receptor adaptor molecule-2; TICAM1 = toll like receptor adaptor molecule-1; TLR4 = toll-like receptor 4) [REVIEW]
Data show that Toll/IL-1R domain-containing adaptor molecule (TICAM)-2 possesses two conserved acidic amino acids, D91 and E92, which regulate TICAM-2 self-activation and signaling.
Findings were SNPs in TICAM2 (P = 3.6 x 10(-6)) and IL1B (P = 4.3 x 10(-5)) associated with TB.
TRAM plays a role in TLR7 signaling through a novel signaling axis towards the activation of anti-viral immunity.
TRAM acts as a sorting adaptor not only for TLR4, but also for TLR2, to facilitate signaling to IRF7 at the endosome, which explains how TLR2 is capable of causing type I IFN induction.
A putative TRAF6-binding motif in TRAM may mediate a new TRAM function in TLR4 signaling in regulating inflammatory responses, distinct from its bridging TLR4 and TRIF. A TRAM E183A mutation abolished this.
results suggest TLR adaptor molecules knockdown, such as MyD88 or TRAM, can decrease IL-6 and IL-8 mRNA and increase CXCL12 mRNA expression in HGF and HPDLF.
The homotypic interaction between TICAM-2 TIR is indispensable to present a scaffold for recruiting the monomeric moiety of the TICAM-1 TIR dimer.
induction of both IL-6 and IL-8 is associated with elevated TIRAP and reduced TRAM mRNA expression
Data indicate that MyD88 works together with the IL-1/IL-18 receptors, can interact with two distinct sorting adaptors, TRAM and Mal, in a conserved manner.
viral inhibitor peptide of TLR4 possibly represents a surface domain of A46 that specifically inhibits TLR4 by masking critical binding sites on MyD88 adaptor-like and TRIF-related adaptor molecule
Overexpression of TIRP activates NF-kappaB and potentiates IL-1 receptor-mediated NF-kappaB activation
the adapter complex of TICAM-2 and TICAM-1 plays a crucial role in lipopolysaccharide-TLR4-mediated activation of IFN-beta
The myristoylation of TRAM targets it to the plasma membrane, where it is essential for LPS responses through the TLR4 signal transduction pathway.
TRAM functions as a sorting adaptor that controls the initiation of TRIF/TICAM1-dependent signaling from an endosomal compartment; TRAM seems to be required for Toll-like receptor-4 coupling on the cell surface to the endosomal activation of TRIF-TRAF3.
TAG is a splice variant of TRAM. TAG inhibits TRAM by displacing TRIF, and TAG overexpression specifically inhibits TLR4 signaling.
TRIF is a downstream protein of TLRs receptors which play a vital role in innate immunity. Expression of TRIF is downregulated in hyperthermia along with inactivation of NF-kappaB pathway.
These data suggest that IPS-1 plays a more important role than TRIF in the early type I IFN response and that both IPS-1 and TRIF are involved at later stages of Zika virus infection.
Experiments with homozygous knockouts of Irakm (encoding a suppressor of MyD88 inactivation) and Trif in competitive bone marrow transplants revealed that MyD88 is required for High Fat Diet expansion of granulocyte macrophage progenitors and that Trif is required for pregranulocyte macrophage progenitor expansion.
Using ovalbumin as model antigen, the authors showed that exposure of dendritic cells to hyperosmolarity strongly inhibits activation of antigen-specific T cells despite enhancement of antigen uptake, processing and presentation. They identified TRIF as key mediator of this phenomenon.
the present study indicated that MyD88 and TRIF blockades serve notable and equivalent roles in protecting cardiac deterioration from severe sepsis by attenuating cytokine release, reducing neutrophil infiltration and alleviating apoptosis.
lipopolysaccharide (LPS) application induces proliferation of dormant hematopoietic stem cells (HSC) and impairs HSC self-renewal via TLR4-TRIF-ROS-p38 signaling.
These results indicate a critical role for Ticam2 in SARS-CoV disease, and highlight the importance of host genetic variation in disease responses.
Distinct mechanisms downstream of TLR4 signaling mediate myelosuppression and hematopoietic stem cell exhaustion during sepsis through unique effects of MyD88 and TRIF.
these data show that both Myd88 and TRIF are necessary for Th17 differentiation in the lungs in response to immunization with lipopolysaccharide
these studies reveal an additional regulatory function of TRIM8 in innate immune responses: TRIM8 catalyzes polyubiquitination of TRIF, resulting in disruption of TRIF-TBK1 interaction
Stimulation of the TLR4-TRIF pathway can protect against the development of allergic airway disease and that a TRIF-dependent adjuvant effect on CD4(+) ICOS(+) T-cell responses may be a contributing mechanism.
Monophosphoryl lipid A stimulation of a TLR4-TRIF-PI3K-Akt pathway prevents lipopolysaccharide-induced ERK activation in the medullar thick ascending limb.
study reporst a key role for TNF/TNFR1 in Yersinia-induced cell death of murine macrophages, which occurs despite the blockade of NF-kappaB and MAPK signaling imposed by Yersinia on infected cells
STING and TRIF Contribute to Mouse Sepsis, Depending on Severity of the Disease Model
the role of Toll-like receptor (TLR) 2, TLR4, myeloid differentiation response gene 88, and Toll-IL-1 receptor domain-containing adaptor-inducing interferon-gamma (TRIF), factors critically involved in the TLR signaling pathway, was studied in experimental autoimmune neuritis.
Juniperus rigida Sieb. extract inhibits macrophage inflammatory responses by attenuating TRIF-dependent signaling and inflammasome activation.
TRIF-independent pathways can be involved in the downregulation of drug metabolizing enzymes and transporters through TLR4 and 3. JNK-dependent mechanisms likely mediate this downregulation.
Data show that annexin A2 (AnxA2) directly exerted negative regulation of inflammatory responses through Toll-like receptor 4 (TLR4)-initiated TRAM protein-TRIF protein pathway occurring on endosomes.
TRIF mediates antibacterial defense during Gram-negative pneumonia, at least in part, by inducing IFN-x03B3; at the primary site of infection.
The authors confirmed that the protective effect of poly I:C against enteric infection of mice with Yersinia enterocolitica was dependent on TLR3-mediated TRIF signaling by using TLR3-deficient mice.
TIRP is a Toll/interleukin-1 receptor (IL1R\; MIM 147810) (TIR) domain-containing adaptor protein involved in Toll receptor signaling (see TLR4\; MIM 603030).
NF-kappa-B-activating protein 502
, TIR domain-containing adapter molecule 2
, TRIF-related adaptor molecule
, cytoplasmic adaptor
, putative NF-kappa-B-activating protein 502
, toll-like receptor adaptor protein 3
, toll/interleukin-1 receptor (TIR) domain-containing adapter protein
, TRIF-related adapter molecule
, TMED7-TICAM2 readthrough
, TIR domain-containing adapter protein
, TRIF-related adapter molecule TRAM
, Toll-interleukin I receptor domain (TIR)-containing adaptor molecule (TICAM) 2
, toll/interleukin-1 receptor domain-containing protein