IkappaBalpha (Tyr-305), phospho-specific polyclonal, anti-human, mouse, rat

Background:
The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins. Activation of IκBα occurs through both serine and tyrosine phosphorylation events. Activation through phosphorylation at Ser-32 and Ser-36 is followed by proteasome-mediated degradation, resulting in the release and nuclear translocation of active NF-κB. This pathway of IκBα regulation occurs in response to various NF-κB-activating agents, such as TNFα, interleukins, LPS, and irradiation. An alternative pathway for IκBα regulation occurs through tyrosine phosphorylation of Tyr-42 and Tyr-305. Tyr-42 is phosphorylated in response to oxidative stress and growth factors. This phosphorylation can lead to degradation of IκBα and NF-κB-activation. In contrast, Tyr-305 phosphorylation by c-Abl has been implicated in IκBα nuclear translocation and inhibition of NF-κB-activation. Thus, tyrosine phosphorylation of IκBα may be an important regulatory mechanism in NF-κB signaling.

Immunogen: IκBα (Tyr-305) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 305 of human IκBα. This peptide sequence has low homology to other IκB proteins.

Specificity: This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose then affinity purified using phospho-IκBα (Tyr-305) peptide (without carrier). The antibody detects a 38 kDa* protein on SDS-PAGE immunoblots of A431 and Jurkat cells treated with pervanadate, but does not detect this band in control cells.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.