TRIAD3A Antibody is Ion exchange chromatography purified.
Immunogen
TRIAD3A antibody was raised against a peptide corresponding to 15 amino acids near the amino-terminus of mouse TRIAD3A. The immunogen is located within amino acids 120 - 170 of TRIAD3A.
RNF216
Reactivity: Human, Mouse, Rat
IF (p)
Host: Rabbit
Polyclonal
AbBy Fluor® 647
Application Notes
TRIAD3A antibody can be used for detection of TRIAD3A by Western blot at 1 to 2 μ,g/mL. Antibody can also be used for immunohistochemistry starting at 10 μ,g/mL. For immunofluorescence start at 20 μ,g/mL.
Antibody validated: Western Blot in mouse samples, Immunohistochemistry in mouse samples and Immunofluorescence in mouse samples. All other applications and species not yet tested.
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
TRIAD3A Antibody is supplied in PBS containing 0.02 % sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C,4 °C
Storage Comment
TRIAD3A antibody can be stored at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
TRIAD3A Antibody: Activation of NF-κ,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.