Recombinant TRIAD1 Monoclonal Antibody (AN302043L)
For research use only.
| Verified Samples | Verified Samples in WB: Jurkat,?293T, Ramos |
| Dilution | WB 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | TRIAD1 |
| Synonyms | ARI, ARIH, TRIAD, ARI2, TRIAD1, ARIH2, HT005, all trans retinoic acid inducible RING finger, Ari 2, Ari-2, Ariadne 2, Ariadne 2 protein homolog, ariadne homolog 2, ariadne homolog 2 (Drosophila), Ariadne RBR E3 ubiquitin protein ligase 2, ARIH 2, E3 ubiquitin protein ligase ARIH2, E3 ubiquitin-protein ligase ARIH2, protein ariadne 2 homolog, Protein ariadne-2 homolog, Triad 1, Triad1 protein, UIP48 |
| Swissprot | |
| Calculated MW | 58 kDa |
| Observed MW |
58 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cytoplasm, Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Epigenetics and Nuclear Signaling, Cell Biology |
| Clone No. | A763 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | 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. 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. 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. |
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