epitope mapping near the N-terminus of SLMAP of human origin
recommended for detection of SLMAP isoforms 1, 2, 3, 6 and 7 of mouse, rat and human origin by WB, IF and ELISA; non cross-reactive with SLMAP isforms 4, 5 or 8; also reactive with additional species, including equine, canine, bovine, porcine and avian
SLMAP Background Information SLMAP (sarcolemmal membrane-associated protein) is a 828 amino acid single-pass type IV membrane protein. Localized to the sacrcolemma in non-replicating cells, SLMAP relocates to centrosomes in a microtubule-dependent manner during cleavage in muscle tissues. SLMAP is thought to be involved in protein-protein interactions, as well as play a role in myoblast fusion. As a homodimeric integral membrane protein, SLMAP has two leucine zippers which form a 77 amino acid coiled-coil structure and contains one forkhead-associated (FHA) domain. Coiled- coil structures may be important for the regulation of neurotransmitter release, N-type calcium channels and membrane fusion, while FHA domains are involved in nuclear signaling. SLMAP exists as eight isoforms produced by alternative splicing.
