RP2 Protein, Human (sf9, GST)

RP2 protein, a GTPase-activating protein (GAP), regulates intracellular trafficking between the Golgi apparatus and the ciliary membrane. It ensures precise localization of proteins like NPHP3 to the cilium membrane by catalyzing GTP ARL3 hydrolysis, leading to UNC119 (or UNC119B) release. RP2 also acts as a GTPase-activating protein for tubulin and a guanine nucleotide dissociation inhibitor for ADP-ribosylation factor-like proteins. In complex with ARL3 and UNC119 (or UNC119B), RP2 directly induces GTP ARL3 hydrolysis, liberating UNC119 (or UNC119B). Interaction is stimulated by activated GTP-bound ARL3. RP2 Protein, Human (sf9, GST) is the recombinant human-derived RP2 protein, expressed by Sf9 insect cells, with N-GST labeled tag. The total length of RP2 Protein, Human (sf9, GST) is 350 a.a., with molecular weight of ~66 kDa.

RP2 protein serves as a GTPase-activating protein (GAP), playing a crucial role in the regulation of intracellular trafficking between the Golgi apparatus and the ciliary membrane. It is involved in the precise localization of proteins, such as NPHP3, to the cilium membrane by catalyzing the hydrolysis of GTP ARL3. This process leads to the subsequent release of UNC119 (or UNC119B). Furthermore, RP2 acts as a GTPase-activating protein for tubulin in conjunction with the tubulin-specific chaperone C, although it does not enhance tubulin heterodimerization. Additionally, RP2 acts as a guanine nucleotide dissociation inhibitor for ADP-ribosylation factor-like proteins. It forms a complex with ARL3 and UNC119 (or UNC119B), where RP2 induces the hydrolysis of GTP ARL3 within the complex, resulting in the liberation of UNC119 (or UNC119B). The interaction with ARL3 is direct and is stimulated by the activated GTP-bound form of ARL3.

Human

Sf9 insect cells

N-GST

O75695 (M1-T350)

6102  [NCBI]

Approximately 66 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.