Product Pathways - Protein Stability
TRIAD1 Antibody #13689
|13689S||100 µl (10 western blots)||---||In Stock||---|
|13689||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||58||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Chicken, Bovine, Dog, Pig, Horse.
Specificity / Sensitivity
TRIAD1 Antibody recognizes endogenous levels of total TRIAD1 protein. Based upon sequence alignment, this antibody is not predicted to cross-react with HHARI/ARIH1.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human TRIAD1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293T cells, transfected with 100 nM SignalSilence® Control siRNA (Unconjugated) #6568 (-) or SignalSilence® TRIAD1 siRNA Ι #13719 (+), using TRIAD1 Antibody (upper) and GAPDH (D16H11) XP® Rabbit mAb #5174 (lower). The TRIAD Antibody confirms silencing of TRIAD1 expression, while the GAPDH (D16H11) XP® Rabbit mAb is used as a loading control.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing Myc/DDK-tagged full-length human TRIAD1 (hTRIAD1-Myc/DDK; +), using TRIAD1 Antibody.
The E3 ubiquitin-protein ligase ARIH2 (TRIAD1) is an Ariadne subfamily ligase involved in the polyubiquitination of proteins designated for proteasomal degradation. The TRIAD1 nuclear protein contains an amino-terminal acidic region, a pair of RING fingers, two carboxyl-terminal coiled coil domains and a novel C6HC DRIL/IBR domain located between the RING fingers. Together, the paired RING fingers and DRIL/IBR domain form a highly conserved TRIAD (two RING fingers and DRIL) domain (1). Research studies suggest that TRIAD1 mediates both Lys48 and Lys63 protein polyubiquitination and acts as a negative regulator of myelopoiesis. TRIAD1 ubiquitin ligase inhibits myeloid cell proliferation by mediating protein ubiquitination through the ubiquitin-conjugating enzymes UbcH7 and UbcH13 (2,3). Experimental deletion of TRIAD1 in mice has a lethal effect, leading to death at the embryonic stage or later due to a severe, multi-organ inflammatory response. Results indicate that TRIAD1 binds IκBβ in dendritic cells and promotes the degradation of the NF-κB inhibitor (4).
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For Research Use Only. Not For Use In Diagnostic Procedures.
XP® is a trademark of Cell Signaling Technology, Inc.
Tween® is a registered trademark of ICI Americas, Inc.
SignalSilence® is a trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.