KappaB ras-1 (κB-ras-1) and kappaB-ras-2 are two small proteins that similar to Ras-like small GTPases that associate with IκB (IκB), an inhibitor of the transcription factor NF-κB. IκB exists in two homologous forms, IκB-alpha and IκB-beta, although IκB-beta contains a unique 47-amino acid region within its ankyrin domain. While inactive IκB-alpha-NF-κB complexes can shuttle in and out of the nucleus, IκB-beta-NF-κB complexes are retained exclusively in the cytoplasm. It is suggested that kappaB-ras proteins preferentially bind to the IκB-beta form through this unique insert within the ankyrin region, thus modulating the cellular location of IκB-beta and regulating the rate of degradation of IκB-beta. This antibody detects both kappaB-ras1 and kappaB-ras2.