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The protein AKT/PKB is a critical regulator of essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. In the present study, we wanted to test if levels of protein AKT changed in in EGF-stimulated epithelial, human breast cancer cell line when treated with varying concentrations of a drug Chondramide (ChB; 30 nM or 100 nM) for different lengths of time (1 or 24 h). Cellular lysate was prepared for each experimental condition, and an equal concentration of protein was loaded into a single lane of the SDS-polyacrylamide gel for each sample. We used western blot to measure the total levels of AKT and the fraction of Akt that is phosphorylated on the serine residue at position 473 (p-AktS473) using a phosphorylation specific antibody. GAPDH was used a loading control. EGF 30 nM ChB 100 nM ChB P-Akers total Akt GAPDH 0 0 + 0 0 1h 0 24h 0 0 0 1h 24h Why do you think the researchers included GAPDH in the figure? ABCD A. B. C. D. Control for cell condition Control for unwanted proteins Positive control for Antibody for AKT Control for amount of protein loaded Indicate for the following statements is they are supported/not supported by the data in the figure. Statement 1. Phosphorylation of AKT (S473) increases upon EGF stimulation Statement 2. The total amount of AKT in the cell reduces upon EGF stimulation_ Statement 3. ChB treatment (both concentration and length of time) increases the amount of phosphorylated AKT.

The protein AKT/PKB is a critical regulator of essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. In the present study, we wanted to test if levels of protein AKT changed in in EGF-stimulated epithelial, human breast cancer cell line when treated with varying concentrations of a drug Chondramide (ChB; 30 nM or 100 nM) for different lengths of time (1 or 24 h). Cellular lysate was prepared for each experimental condition, and an equal concentration of protein was loaded into a single lane of the SDS-polyacrylamide gel for each sample. We used western blot to measure the total levels of AKT and the fraction of Akt that is phosphorylated on the serine residue at position 473 (p-AktS473) using a phosphorylation specific antibody. GAPDH was used a loading control. EGF 30 nM ChB 100 nM ChB P-Akers total Akt GAPDH 0 0 + 0 0 1h 0 24h 0 0 0 1h 24h Why do you think the researchers included GAPDH in the figure? ABCD A. B. C. D. Control for cell condition Control for unwanted proteins Positive control for Antibody for AKT Control for amount of protein loaded Indicate for the following statements is they are supported/not supported by the data in the figure. Statement 1. Phosphorylation of AKT (S473) increases upon EGF stimulation Statement 2. The total amount of AKT in the cell reduces upon EGF stimulation_ Statement 3. ChB treatment (both concentration and length of time) increases the amount of phosphorylated AKT.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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The protein AKT/PKB is a critical regulator of essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. In the present study, we wanted to test if levels of protein AKT changed in in EGF-stimulated epithelial, human breast cancer cell line when treated with varying concentrations of a drug Chondramide (ChB; 30 nM or 100 nM) for different lengths of time (1 or 24 h). Cellular lysate was prepared for each experimental condition, and an equal concentration of protein was loaded into a single lane of the SDS-polyacrylamide gel for each sample. We used western blot to measure the total levels of AKT and the fraction of Akt that is phosphorylated on the serine residue at position 473 (p-AktS473) using a phosphorylation specific antibody. GAPDH was used a loading control. EGF 30 nM ChB 100 nM ChB P-Ak47 total Akt GAPDH 0 0 + 0 0 0 0 0 1h 24h 1h 24h 0 Why do you think the researchers included GAPDH in the figure? A. B. C. D. Control for cell condition Control for unwanted proteins Positive control for Antibody for AKT Control for amount of protein loaded Indicate for the following statements is they are supported/not supported by the data in the figure. Statement 1. Phosphorylation of AKT (S473) increases upon EGF stimulation Statement 2. The total amount of AKT in the cell reduces upon EGF stimulation_ Statement 3. ChB treatment (both concentration and length of time) increases the amount of phosphorylated AKT.
Transcribed Image Text:The protein AKT/PKB is a critical regulator of essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. In the present study, we wanted to test if levels of protein AKT changed in in EGF-stimulated epithelial, human breast cancer cell line when treated with varying concentrations of a drug Chondramide (ChB; 30 nM or 100 nM) for different lengths of time (1 or 24 h). Cellular lysate was prepared for each experimental condition, and an equal concentration of protein was loaded into a single lane of the SDS-polyacrylamide gel for each sample. We used western blot to measure the total levels of AKT and the fraction of Akt that is phosphorylated on the serine residue at position 473 (p-AktS473) using a phosphorylation specific antibody. GAPDH was used a loading control. EGF 30 nM ChB 100 nM ChB P-Ak47 total Akt GAPDH 0 0 + 0 0 0 0 0 1h 24h 1h 24h 0 Why do you think the researchers included GAPDH in the figure? A. B. C. D. Control for cell condition Control for unwanted proteins Positive control for Antibody for AKT Control for amount of protein loaded Indicate for the following statements is they are supported/not supported by the data in the figure. Statement 1. Phosphorylation of AKT (S473) increases upon EGF stimulation Statement 2. The total amount of AKT in the cell reduces upon EGF stimulation_ Statement 3. ChB treatment (both concentration and length of time) increases the amount of phosphorylated AKT.
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