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Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Additionally we are shipping TIFA Proteins (8) and many more products for this protein.
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TIFA expression limited proliferation of multiple myeloma cancer cells. In conclusion these results indicate that TIFA functions as a key transducer in DNA damage-induced NF-kappaB activation
TIFA may serve as a biomarker in the prediction of lung adenocarcinoma. Furthermore, TIFA may modulate lung cancer cell survival and proliferation through regulating the synthesis of apoptosis-associated proteins.
TIFA is a crucial mediator in the endothelial innate immune response by potentiating and amplifying NLRP3 inflammasome via augmenting signals 1 and 2
study revealed that host TIFA and H. pylori-derived heptose-1,7-bisphosphate are critical effectors of innate immune signaling that account for much of the inflammatory response to H. pylori in gastric epithelial cells
These results define TIFA as a rheostat for intracellular bacterial replication, escalating the immune response to invasive Gram-negative bacteria that exploit the host cytosol for growth.
we report that Aurora A is essential for phosphorylation of the TRAF-interacting protein TIFA
This study reports the crystal structures of TIFA (residues 1-150, with the unstructured C-terminal tail truncated) and its complex with the N-terminal phosphothreonine9 peptide (residues 1-15).
an innate immune signaling axis, mediated by phosphorylation-dependent oligomerization of the TRAF-interacting protein with forkhead-associated domain (TIFA) that is triggered by heptose-1,7-bisphosphate.
identify a novel threonine phosphorylation site on TIFA and show that this phosphorylated threonine binds with the FHA domain of TIFA, leading to TIFA oligomerization and TIFA-mediated NF-kappaB activation
TIFA induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism
The increase in TIFA level appears to be a feed-forward mechanism involved in TLR4/MyD88-dependent signaling, leading to NF-kappaB activation and HMGB1 release
TIFA is likely to mediate IRAK-1/TRAF6 interaction upon IL-1 stimulation
We propose that ZCCHC11 is a unique TLR signal regulator, which interacts with TIFA after LPS treatment and suppresses the TRAF6-dependent activation of NF-kappaB.
Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (By similarity).
TRAF-interacting protein with forkhead-associated domain
, TRAF-interacting protein with a forkhead-associated domain
, TRAF-interacting protein with FHA domain-containing protein A
, TRAF6-binding protein
, TRAF2 binding protein
, TRAF2-binding protein
, TRAF6 binding protein
, putative MAPK-activating protein PM14
, putative NF-kappa-B-activating protein 20
, Traf2 binding protein