Anti-ARF1+ARF3 antibody [EPR8304(B)] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ARF1 and ARF3 are small GTP-binding proteins part of the ADP-ribosylation factor (ARF) family involved in vesicle formation and trafficking. Alternate names for these proteins include ADP-ribosylation factor 1 and 3. ARF1 has a molecular mass of about 21 kDa and ARF3 is similar in size. These proteins localize primarily to the Golgi apparatus and cytoplasmic regions including the endoplasmic reticulum and plasma membrane. The expression of ARF1 and ARF3 is widespread occurring in various cell types across different tissues indicating roles in fundamental cellular processes.

Biological function summary

ARF1 and ARF3 regulate the assembly of coat protein complexes on membrane surfaces which is essential for vesicle formation. They participate in the transport of proteins and lipids between cellular organelles particularly in the secretory and endocytic pathways. ARF1 specifically functions in activating phospholipase D and is part of large protein complexes that involve coatomer proteins and clathrin. While they share overlapping functions ARF1 and ARF3 exhibit some distinct roles in vesicle trafficking indicating the specificity in biological functions.

Pathways

ARF1 and ARF3 play important roles in the regulation of the Golgi apparatus and endocytic pathways. They are important in coordinating vesicular transport by interacting with proteins such as COPI and clathrin facilitating cargo sorting and trafficking. ARF1 is also linked to the phosphoinositide metabolic pathway influencing membrane dynamics and trafficking processes. Whereas ARF3 is involved in pathways that modulate cytoskeletal functions indicating its diverse effects within related cellular signaling and trafficking pathways.

Associated diseases and disorders

Defects in ARF1 and ARF3 functions can contribute to conditions such as cancer and neurodegenerative diseases. Aberrant ARF1 expression has connections to cancer progression due to its influence on cell migration and invasion possibly linked with proteins like clathrin that modulate vesicular trafficking. Altered ARF3 activity associates with neurodegenerative disorders involving connections with proteins in signaling pathways related to ARF1 impacting neuronal transport and synaptic functions. These proteins' involvement in cellular trafficking highlights their roles in maintaining cellular homeostasis and their links to disease states.