The mechanism of vesicular trafficking is a process that is not well understood, but it is critical to the operation and function of a cell. Rab proteins guide anterograde (ER to plasma membrane) and retrograde (plasma membrane to ER) directional vesicular movement, but most Rab proteins have been shown to have varying trafficking roles with membrane-bound vesicle movement, tethering, and fusion specific to the cargo within the vesicle. This study aimed to identify Rab proteins that are involved in anterograde trafficking of human gonadotropin-releasing hormone receptor (GnRHR). Plasmids encoding Rab GTPase DNA, along with human GnRHR DNA, were transfected into Cos-7 African green monkey kidney tumor cells in vitro. Cells were grown in tritium inositol and upon stimulation of GnRHR, inositol phosphates (IP) containing radioactive markers were synthesized. A radioimmunoassay was conducted to determine total presence of inositol phosphate (IP), a marker that correlates with GnRHR presence at the plasma membrane. Rab6 and Rab3a were identified as significantly increasing IP levels, an indication of higher presence of GnRHR at the cell membrane and anterograde activity. Moving forward, further research will be pursued to find additional Rab GTPase proteins involved in anterograde trafficking and their specific function and localization. Understanding the pathway of GnRHR to the plasma membrane could improve therapeutic treatments for hypogonadotropic hypogonadism, a disease caused by loss-of-function of GnRHR due to a failure of expression at the cell membrane.