I am studying the subcellular localization of a protein. To see if a GFP fusion protein can be compared to the native protein, I fused GFP to the N-terminal of the protein. In my western blots and confocal images I can see this fusion seems to show that GFP is cleaved off. My protein construct looks basically like this: GFP-Signal Peptide of protein-Rest of protein coding sequence. My question is whether the signal peptide can still be recognized and cleaved? I can't find much literature on the topic as many people insert GFP downstream of the SP. Any info will be greatly appreciated