Ring finger protein 138
| Catalog# | Product Description | Host Species | Nature | Cross reactivity | Quantity | Volume | Price |
|---|---|---|---|---|---|---|---|
| TRIF-101AP | TRIF antibodies | Rabbit | AP | r, m, h | 100.0 ug | 150-500 ul |
$245.00
|
| FITC-TRIF | FITC-conjugated antibodies | Rabbit | FITC-AP | r, m, h | 100.0 ug | 150-500 ul |
$350.00
|
| P-TRIF | Antigenic blocking peptide | n/a | Synthetic peptide | n/a | 250.0 ug | 100 ul |
$125.00
|
| PC-TRIF | WB positive control for TRIF | n/a | Prtoein in ready-to-use buffer | n/a | 0.0 ug | 150 ul |
$185.00
|
During the development of immunity, Toll like receptors (TLRs) are activated by adjuvants and reveal molecular mechanisms by which different ligands are recognized by the same receptor in different shapes. Among various ligands that activated TLR are deoxycytidylate-phosphoate-deoxy guanylate (CpGp)DNA, which activate TLR and monophopshoryl lipid A, derived from bacterial endotoxin, to activate TLR 4. The recognition of lipidA by TLR 4 requires MD-2 which binds to extracellular domain on TLR 4. This TLR4-MD2 complex then reorganizes the TIR domain of the TLR4 enabling the recruitment of 4 adapter molecules, MyD88, TRIF (also known as TICAM1) and TRAM (also known as TICAM2). Interaction of these adapter molecules initiate the signal transduction cascade that led the production and secretion of molecules that regulate immune response as well as enhance the cell surface expression of molecules on specialized immune cells (dentritic cells) that enhance binding of T cells. The mechanism of immune response diversification though not fully understood, is partly explained by the way TLR-MD-2 complexes alter the TIR domain via the adapter molecules. The variations in the signaling pathways differ either TRAM or TRIF are activated and or Mal and MyD88 pathways are activated. The TRIF and TRAM activation results in INF-b induced activation of T cells that modulate the immune response and Mal and MyD88 activation resulted in NFkb and cytokine release that led to inflammation and harm to the host (1).
The transcript for mouse TRIF are clustered into 33,409 “transcriptional units” of these transcriptional units which exhibit high degree of alternate splicing about 4000 are new protein-coding and 11665 are new non coding regions. TRIF gene is one of the many new transcriptional unit new protein. TRIF is a highly conserved protein in various species ranging in 209 -279 amino acids. TRIF contains a RING domain of 40-60 amino acids that bind 2 atoms of zinc by cross brace motif is involved in protein-protein interactions that is necessary for signal transduction, development and replication (2).
The TRIF/TICAM 1-selective antibodies were generated against peptide form unique region of the TIRF/TICAM 1 protein sequence that is not present in other adapter molecules. FabGennix Inc. has generated epitope specific rabbit anti-TRIF/TICAM 1 rabbit polyclonal (mono-specific to their epitope specificity) antibodies utilizing linear and cyclic peptide sequences. These antibodies have been fully characterized for cross reactivity with other members of the TIR adapter molecules and with cellular proteins using Western blot analyses. Limited quantities of the antigenic blocking peptide for TRIF/TICAM1 antibody is also available (inquire for availability). FabGennix has generated antibodies to TOL-receptors and most of the interacting protein targets, for a complete listing visit www.Fabgennix.com. FabGennix will label these antibodies to fluorophores, enzymes and other reporting molecules at nominal charge.
For research use only, not for diagnostic or therapeutic use.
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