Background:  A cytoplasmic domain of approximately 80 amino acids has been identified in the apoptosis-mediating receptors of TNF-R1 and FAS. This region was determined to be necessary for the transduction of the apoptotic signal and was designated the “death domain”. Other death domain-containing, but otherwise structurally unrelated, proteins were identified on the basis of their ability to associate with the cytoplasmic domains of TNF-R1 or FAS. The receptor interacting protein RIP is a death domain-containing serine/threonine kinase which associates with FAS or the TNF-R1 binding protein TRADD. RAIDD (RIP-associated ICH-1/Ced-3 homologous protein with a death domain) has been identified as a RIP binding protein that also associates with members of the caspase family, providing a link between activation of the TNF-Rs and the triggering of the cysteine protease cascade. The amino-terminal domain of RAIDD shares significant homology with the prodomain of ICH-1 and mediates the binding of RAIDD to this cysteine protease.

Description: Rabbit polyclonal to RAIDD

Immunogen: KLH conjugated synthetic peptide derived from RAIDD

Specificity:  ·Reacts with Human, Mouse, Pig, Dog and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 23 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.