GRP1 (K400) polyclonal antibody

GRP1 (general receptor for phosphoinositides-1) contains a Pleckstrin homology (PH) domain as well as a Sec7 domain. The PH domain has high binding affinity for phosphatidylinositol 3,4,5-trisphosphate Ptdlns(3,4,5)P3), while the Sec7 homology domain is responsible for catalyzing guanine nucleotide exchange of ADP-ribosylation factor (ARF) proteins. GRP1 co-localizes with ARF6 and catalyzes GTP/GDP exchange on ARF6. It is known to interact with Ptdlns(3,4,5)P3 localized to the plasma membrane in vitro and may also be a Ptdlns(3,4,5)P3 receptor. Additionally, GRP1 may regulate protein sorting and membrane trafficking through interaction with the guanosine triphosphate ARF, and may control cell adhesion through interaction with integrins.