Recombinant Human ARF1 protein

**Background of ARF1 Recombinant Protein**

ADP-ribosylation factor 1 (ARF1) is a small GTP-binding protein belonging to the Ras superfamily of GTPases. It plays a pivotal role in intracellular vesicular trafficking, particularly in the formation of COP I-coated vesicles, which mediate retrograde transport between the Golgi apparatus and the endoplasmic reticulum. ARF1 cycles between an inactive GDP-bound state and an active GTP-bound state, a process regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Upon activation, ARF1 recruits coat proteins and lipid-modifying enzymes to membranes, facilitating cargo sorting, membrane curvature, and vesicle budding.

Recombinant ARF1 protein is engineered using heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce purified, functional ARF1 for biochemical and structural studies. This recombinant form retains the ability to bind GTP/GDP and interact with effector molecules, making it a vital tool for dissecting ARF1’s role in membrane trafficking, organelle maintenance, and signal transduction. Researchers use it to study ARF1’s involvement in diseases, including cancer (e.g., aberrant secretion pathways) and neurodegenerative disorders (e.g., disrupted protein trafficking).

Additionally, recombinant ARF1 enables screening for small-molecule inhibitors or activators targeting its regulatory cycle, offering therapeutic potential. Its structural characterization via X-ray crystallography or cryo-EM has provided insights into GTPase conformational changes and interaction interfaces. Overall, ARF1 recombinant protein serves as a cornerstone for understanding cellular logistics and developing targeted interventions in trafficking-related pathologies.