• BCRP consists of 655 amino acids and possesses six transmembrane helices and one ATP­ binding site. Because BCRP is a half­-transporter, current evidence suggests that homodimerization or multimerization is required for transporter activity as illustrated. 
• The exons 2~16 of rat Bcrp gene were knocked out in B-Bcrp KO rats, resulting in a disruption of the Bcrp gene.
• Bcrp mRNA and protein were detectable only in wild-type SD rats, but not in B-Bcrp KO rats. 

• Applicable for investigating ATP-powered transport proteins in physiological drug distribution.

Bcrp mRNA expression in wild-type SD rats and B-Bcrp KO rats by RT-PCR. Kidney, brain and liver RNA were isolated from wild-type SD rats (+/+) and B-Bcrp KO rats (-/-), then cDNA libraries were synthesized by reverse transcription, followed by PCR with rat Bcrp primers. Rat Bcrp mRNA was detectable only in wild-type SD rats, but not in B-Bcrp KO rats.

Western blot analysis of BCRP protein expression in B-Bcrp KO rats. Various tissue lysates were collected from wild-type SD rats (+/+) and B-Bcrp KO rats (-/-), and then analyzed by western blot with anti-BCRP antibody (abcam, ab207732). 40 μg total proteins were loaded for western blotting analysis. BCRP was not detectable in B-Bcrp KO rats.