Background

The immunosuppressant drug cyclosporin A blocks a calcium-dependent signal from the T-cell receptor (TCR) that normally leads to T-cell activation. When bound to cyclophilin B, cyclosporin A binds and inactivates the key signaling intermediate calcineurin. The protein encoded by this gene functions similarly to cyclosporin A, binding to cyclophilin B and acting downstream of the TCR and upstream of calcineurin by causing an influx of calcium. This integral membrane protein appears to be a new participant in the calcium signal transduction pathway, implicating cyclophilin B in calcium signaling, even in the absence of cyclosporin.

Images

Western blotting analysis using anti-calcium modulating ligand antibody (Cat#63803). Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with anti-calcium modulating ligand antibody (Cat#63803, 1:2,500) and HRP-conjugated goat anti-mouse secondary antibody (Cat#101, 1:20,000) respectively. Image was developed using FeQTM ECL Substrate Kit (Cat#226).

Western blotting analysis using anti-calcium modulating ligand antibody (Cat#63803). Calcium modulating ligand expression in wild type (WT) and calcium modulating ligand (CAMLG) shRNA knockdown (KD) HeLa cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with anti-calcium modulating ligand antibody (Cat#63803, 1:5,000) and HRP-conjugated goat anti-mouse secondary antibody (Cat#101, 1:20,000) respectively. Image was developed using NaQ™ ECL Substrate Kit (Cat#716).

You may also be interested in: