Touch sensing is essential to human communication, quality of life and health; however, the underlying molecular mechanisms remain mostly unknown. Touch is mediated by ion channels on sensory neurons, such as Transient receptor potential (TRP) channels. Recently drosophila’s mechanosensory TRP channel, No mechanoreceptor potential C (NOMPC) has been illuminated as a possible direct gating ion channel that transduces mechanical stimuli into electrical and chemical signals by opening its ion pore. Here, we first demonstrate features of NOMPC using total internal reflection fluorescence (TIRF) microscopy and magnetic tweezer. We showed the stable tetrameric formation by bleaching the eGFP-NOMPC recombinant protein with laser on TIRF microscopy. Also we pulled eGFP-NOMPC-Spytag recombinant protein using magnetic tweezer to discover the mechanical characteristics of NOMPC. Ours study established the preliminary experimental environments to understanding the unexplored mechanism of NOMPC.