The SLC4A1 (Band 3) protein is the most abundant integral protein of human erythrocyte membranes and functions as the major anion transporter polypeptide of erythrocytes. SLC4A1 is a 90-100 kDa protein, its microheterogeneity is ascribed mainly to the structural heterogeneity of the carbohydrate moiety. The C-terminal portion of the molecule spans the membrane several times, and is responsible for anion transport. The N-terminal portion, comprising almost half of the polypeptide chain of SLC4A1, is located inside the red cell and interacts with cytoskeletal and cytoplasmic proteins such as ankyrin.

Strain specific hCD233/SLC4A1 expression analysis in homozygous B-hSLC4A1 mice(H/H) by flow cytometry. Blood were collected from wild-type C57BL/6N mice(+/+) and B-hSLC4A1 mice(H/H) , and analyzed by flow cytometry with anti-human CD233/SLC4A1 antibody (Miltenyi biotec, 130-117-825). Human CD233/SLC4A1 was detectable in homozygous B-hSLC4A1 mice.

Strain specific analysis of SLC4A1 mRNA expression in wild-type C57BL/6N mice and B-hSLC4A1 mice by RT-PCR. Kidney RNA were isolated from wild-type C57BL/6N mice (+/+) and homozygous B-hSLC4A1 mice (H/H), then cDNA libraries were synthesized by reverse transcription, followed by PCR with mouse or human SLC4A1 primers. Mouse Slc4a1 mRNA was detectable in wild-type mice. Human SLC4A1 mRNA was detectable only in homozygous B-hSLC4A1 mice(H/H) but not in wild-type mice.