Anti-Integrin β4 (Tyr-1526), Phosphospecific Antibody

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.

Our Integrin β4 (Tyr-1526) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat Integrin β4 (Tyr-1526) and is antigen affinity purified. It is great for use in WB, ICC.

Phospho-Integrin β4 (Tyr-1526) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 1526 of human Integrin β4. This peptide sequence is found in all three Integrin β4 isoforms and is highly conserved in rat and mouse Integrin β4.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose and to unphosphorylated Integrin β4 (Tyr-1526) peptide before affinity purification using phospho-Integrin β4 (Tyr-1526) peptide (without carrier) . The purified antibody detects a 200kDa* protein corresponding to the molecular mass of Integrin β4 on SDS-PAGE immunoblots of A431 and src-transformed Hct116 cells treated with pervanadate, but not in control cells.