Anti cullin1 antibody

A549 cells were treated with 1 µmol/L MLN4924 for either 12 h or 24 h. As a control, an equal volume of DMSO was added. Cells from each group were collected, lysed with sodium dodecyl sulfate buffer, and heated at 100 °C for 10 min. Proteins were separated on 10% Bis–Tris polyacrylamide gels by electrophoresis and transferred to polyvinylidene fluoride membranes (Millipore, Bedford, USA). Protein bands were visualized using an enhanced chemiluminescence kit and images were captured using an Amersham Imager 680 (GE Healthcare, IL, USA). Anti-Cullin1 antibody (Abcam, Cambridge, United Kingdom, 75817), anti-phosphorylated nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha (p-IκBα) (Cell Signaling Technology, MA, USA, 2859), anti-IκBα (Cell Signaling Technology, MA, USA, 9242) and anti-β-actin antibody (HuaAn, M1210-2) were purchased.

A549 cells were treated with 1 µmol/L MLN4924 for either 12 h or 24 h. As a control, an equal volume of DMSO was added. Cells from each group were collected, lysed with sodium dodecyl sulfate buffer, and heated at 100 °C for 10 min. Proteins were separated on 10% Bis–Tris polyacrylamide gels by electrophoresis and transferred to polyvinylidene fluoride membranes (Millipore, Bedford, USA). Protein bands were visualized using an enhanced chemiluminescence kit and images were captured using an Amersham Imager 680 (GE Healthcare, IL, USA). Anti-Cullin1 antibody (Abcam, Cambridge, United Kingdom, 75817), anti-phosphorylated nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha (p-IκBα) (Cell Signaling Technology, MA, USA, 2859), anti-IκBα (Cell Signaling Technology, MA, USA, 9242) and anti-β-actin antibody (HuaAn, M1210-2) were purchased.