KappaB ras-1 (kappaB-ras-1) and kappaB-ras-2 are two small proteins that similar to Ras-like small GTPases that associate with IkappaB (IkappaB), an inhibitor of the transcription factor NF-kappaB. IkappaB exists in two homologous forms, IkappaB-alpha and IkappaB-beta, although IkappaB-beta contains a unique 47-amino acid region within its ankyrin domain. While inactive IkappaB-alpha-NF-kappaB complexes can shuttle in and out of the nucleus, IkappaB-beta-NF-kappaB complexes are retained exclusively in the cytoplasm. It is suggested that kappaB-ras proteins preferentially bind to the IkappaB-beta form through this unique insert within the ankyrin region, thus modulating the cellular location of IkappaB-beta and regulating the rate of degradation of IkappaB-beta. This antibody is specific for kappaB-ras1 and has no cross-reactivity to kappaB-ras2.
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