Purity: > 85% by SDS - PAGE Format: Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 10% glycerol . 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. CAMLG 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. Recombinant human CAMLG protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.