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|Tested species reactivity||Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic peptide corresponding to 15 residues near the N-terminus of mouse TRIAD3A.|
|Purification||Antigen affinity chromatography|
|Contains||0.02% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
A suggested positive control for this product is testis or peripheral blood leukocytes.
Activation of NF-?B as a result of Toll-like receptor (TLR) and IL-1 receptor signaling is a major component of innate immune responses. Signals from these receptors are relayed by a number of adapter molecules such as TRIF, TIRAP, and MyD88. Several regulatory mechanisms exist to control TLR signal transduction, including the inhibition of TLR expression and signaling by molecules such as ST2 and SIGIRR. Another mechanism is by the ubi-quitinization of selected TLRs by TRIAD3A, an E3 ubiquitin-protein ligase. TRIAD3A is a RING finger protein that can bind to TLR4 and TLR9, and to a lesser extent TLR3 and TLR5, catalyzing the ubiquitization of these molecules. Overexpression of TRIAD3A promoted the nearly complete degradation of TLR4 and TLR9; this reduction was reflected in the decreased signal-specific activation by ligands specific for these TLRs. Conversely, depletion of TRIAD3A resulted in enhanced TLR activation.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
2810055G22Rik; AI647468; AU019462; C86502; E3 ubiquitin ligase; E3 ubiquitin-protein ligase RNF216; F830018F18Rik; triad domain-containing protein 3; TRIAD3; Ubce7ip1; ubcM4-interacting protein 83; ubiquitin-conjugating enzyme 7-interacting protein 1; UIP83
2810055G22Rik; AI647468; AU019462; C86502; F830018F18Rik; Rnf216; TRIAD3; Ubce7ip1; UIP83; Zin