GDI2 is a ubiquitously expressed protein that functions by slowing the rate of dissociation of GDP from Rab proteins and releasing GDP from membrane-bound Rabs . This regulation is essential for maintaining the proper function of intracellular membrane trafficking. The protein prevents the GDP to GTP exchange of most Rab proteins, keeping these small GTPases in their inactive GDP-bound form . This regulation is critical for various cellular processes, including protein transport to the cilium and ciliogenesis .
The GDI2 gene is located on chromosome 10 and contains many repetitive elements, indicating that it may be prone to inversion/deletion rearrangements . Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms . The gene is associated with several pathways, including the innate immune system and vesicle-mediated transport .
Recombinant Human GDI2 is typically produced in E. coli and is available with an N-terminal His-tag, corresponding to the amino acids 1-445 of the human GDI2 . The recombinant protein is used in various research applications, including studies on vesicular trafficking and intracellular membrane dynamics. It is important to note that recombinant GDI2 is for research use only and is not approved for use in humans or clinical diagnosis .
GDI2 is a valuable tool in research focused on understanding the mechanisms of intracellular trafficking and the role of Rab proteins in cellular processes. Its ability to regulate the GDP-GTP exchange reaction makes it a critical component in studies related to vesicular transport and membrane dynamics.