Mouse IKK beta Antibody

Detection of Mouse IKK beta by Western Blot.

Western blot shows lysates of BaF3 mouse pro-B cell line. PVDF membrane was probed with 0.5 µg/mL of Rat Anti-Mouse IKK beta Monoclonal Antibody (Catalog # MAB7155) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody. A specific band was detected for IKK beta at approximately 87 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

Detection of IKK beta by Western Blot

IL-3-induced IKK activation was not associated with the degradation of I kappaB-alpha followed by nuclear translocation of p65. (A) Phosphorylation of IKKs after IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 cells were stimulated with IL-3 for the indicated times, and whole-cell lysates were immunoblotted using the indicated Abs. Long and short exposures to detect phosphorylated IKK1 and IKK2 are shown. An arrowhead indicates the band corresponding to phosphorylated IKK1 at 5 min after IL-3 stimulation. A dagger denotes the detection of IKK2 by potential cross-reactivity of the anti-IKK1 Ab. (B) Phosphorylation of IKKs in IKK KO cells after IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 parental (WT), IKK1 KO, IKK2 KO, and IKK1/2 DKO cells were stimulated with IL-3 for 5 min. Immunoblot analysis was performed with whole-cell lysates using the indicated Abs. Arrowheads indicate the bands corresponding to phosphorylated IKK1. (C) Degradation of I kappaB-alpha by TNF-alpha but not by IL-3 stimulation. Following IL-3 deprivation, Ba/F3 cells were stimulated with IL-3 or TNF-alpha for the indicated durations, and whole-cell lysates were immunoblotted using the indicated Abs. (D) Induction of nuclear translocation of p65 by TNF-alpha but not by IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 cells were stimulated with IL-3 or TNF-alpha for the indicated times and immunoblotted with Abs to the cytosol marker alpha-tubulin and the nuclear marker fibrillarin. Long and short exposures to detect p65 are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35563758), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of IKK beta by Western Blot

IL-3-induced IKK activation was not associated with the degradation of I kappaB-alpha followed by nuclear translocation of p65. (A) Phosphorylation of IKKs after IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 cells were stimulated with IL-3 for the indicated times, and whole-cell lysates were immunoblotted using the indicated Abs. Long and short exposures to detect phosphorylated IKK1 and IKK2 are shown. An arrowhead indicates the band corresponding to phosphorylated IKK1 at 5 min after IL-3 stimulation. A dagger denotes the detection of IKK2 by potential cross-reactivity of the anti-IKK1 Ab. (B) Phosphorylation of IKKs in IKK KO cells after IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 parental (WT), IKK1 KO, IKK2 KO, and IKK1/2 DKO cells were stimulated with IL-3 for 5 min. Immunoblot analysis was performed with whole-cell lysates using the indicated Abs. Arrowheads indicate the bands corresponding to phosphorylated IKK1. (C) Degradation of I kappaB-alpha by TNF-alpha but not by IL-3 stimulation. Following IL-3 deprivation, Ba/F3 cells were stimulated with IL-3 or TNF-alpha for the indicated durations, and whole-cell lysates were immunoblotted using the indicated Abs. (D) Induction of nuclear translocation of p65 by TNF-alpha but not by IL-3 stimulation. Following IL-3 deprivation for 6 h, Ba/F3 cells were stimulated with IL-3 or TNF-alpha for the indicated times and immunoblotted with Abs to the cytosol marker alpha-tubulin and the nuclear marker fibrillarin. Long and short exposures to detect p65 are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35563758), licensed under a CC-BY license. Not internally tested by R&D Systems.