It’s been found that many newly synthesized proteins are transferred along the biosynthetic pathway within an ineffective method. As an example, within the GPCR class, only 50% of the newly synthesized Vortioxetine opioid receptors are sent to the plasma membrane. The fate of the newly synthesized GPCR results in the interactions with a few specialized proteins, generically called molecular chaperones. These molecular chaperones are heterogeneous, with different subcellular localization and have different effects around the chaperoned protein, like improving the status and favoring the transportation, or determining intracellular storage and proteasomal degradation. Thus, it is not surprising that interfering with the activity or expression of different molecular chaperones is found to change the rate of intracellular transport for many proteins. Also, downregulation of the cellular levels of AHSA1, a HSP90 company chaperone, improved the cell surface of CFTR 508 mutant. In contrast, Infectious causes of cancer inhibition of HSP90 activity reduced the maturation rate of insulin receptor and nicotinic receptors. Currently few certain pharamacological agents are available to regulate the action of molecular chaperones. This deficit is partially compensated by several non-specific compounds, called pharmacological chaperones, which were shown to strengthen the misfolded proteins and allow their development within the biosynthetic pathway. The non specific medicinal chaperones are including osmolytes, inhibitors of sarco reticulum Ca2 ATP ase and facets enhancing the heat shock response. Interestingly, contact with low-temperature in addition has been proposed to function in the same way as non-specific medicinal chaperones, improving the subcellular transfer of CFTR 508 mutant and potassium channels individual ether a spin gorelated gene channels. Understanding the mechanisms regulating the intracellular trafficking of specific proteins Tipifarnib clinical trial can offer new therapeutic methods to a few diseases brought on by accumulation of misfolded proteins. Consequently, in the present work we studied the subcellular localization of 2C AR at low temperature and at 37 C and we investigated the mechanisms underlying the specific receptor intracellular trafficking. The non specific binding established in presence of non radioactive rauwolscine showed less than a large number of the total radioactivity and it absolutely was subtracted from the results. In preliminary experiments we discovered that performing the binding process at lowtemperature stops RX821002 internalization. This is tested, by washing three times to the cells with 50 mM glycine to remove plasma membrane bound radioactivity. Eventually the cells were trypsinized and fractionated using Qproteome cell compartment kit and the radioactivity was determined in each portion.