Attach few signal recognition amino acids to the N terminal end of your peptide, eithr bind it to serine residues or lysine or any other aromatic amino acids., it will satrt signalling. 

What do you mean? Express two variants of the same protein (each with a different signal peptide) or a single variant with two signal peptides in tandem?

Thank you for both answer. Alejando I like to express a single variant with two signal peptides in tandem. Is that a problem?. The secreted protein will have signal peptide or both signal peptides will be cut?.

Thank you

I honestly don't have a clue, but I would expect it would cause trouble. The problem is that signal peptides are hydrophobic, hence if only the first peptide is removed, the remaining one may interfere with proper folding or act as a membrane anchor. In either case you would not observe secretion into the medium. On the other hand, signal peptide length varies within very narrow limits due to constrains imposed by the physical characteristics of the secretion machinery, so I do not see how cleavage would take place directly at the end of the second peptide.

But what do I know. Perhaps they may be cut sequentially. Why don't you analyze your sequence design using something like SignalP?