Double stranded RNA (dsRNA) generated by most viruses during the infectious cycle is a potent stimulator of interferons. Interferons bind to cell surface receptors and stimulate the synthesis of several proteins that interfere with viral replication. One protein, 2'5'-oligo-adenylate synthetase, indirectly activates an endoribonuclease that degrades viral RNA. Another protein, p68 serine/threonine protein kinase (also known as PKR and TIK), is induced following interferon stimulation and activated by autophosphorylation in the presence of dsRNA. Upon activation, p68 phosphorylates the α subunit of the eukaryotic initiation factor 2 (eIF-2) resulting in inhibition of protein synthesis and, in turn, inhibition of viral replication. Evidence also suggests that p68 protein kinase inhibits proliferation and potentiates tumor suppressor function. In addition, p68 has been shown to phosphorylate Iκ-B, thus activating NF-κB which induces interferon-β gene transcription.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.