Anti-CAMLG Antibody Picoband® PE Conjugated

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.

A synthetic peptide corresponding to a sequence in the middle region of human CAMLG. Human CAMLG shares 91.7% and 95.7% amino acid (aa) sequence identity with mouse and rat CAMLG, respectively.

1. Bram, R. J., Crabtree, G. R. Calcium signalling in T cells stimulated by a cyclophilin B-binding protein. Nature 371: 355-358, 1994. 2. Bram, R. J., Valentine, V., Shapiro, D. N., Jenkins, N. A., Gilbert, D. J., Copeland, N. G. The gene for calcium-modulating cyclophilin ligand (CAMLG) is located on human chromosome 5q23 and a syntenic region of mouse chromosome 13. Genomics 31: 257-260, 1996. 3. Guo, S., Lopez-Ilasaca, M., Dzau, V. J. Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of angiotensin II-mediated nuclear factor of activated T cells (NFAT) activation. J. Biol. Chem. 280: 12536-12541, 2005.