GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs . Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis . Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport . Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins . RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation . Required for normal progress through mitosis . The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules . Acts as a negative regulator of the kinase activity of VRK1 and VRK2 . Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases . .

p62826

GTP-binding nuclear protein Ran (EC 3.6.5.-) (Androgen receptor-associated protein 24) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein),RAN ARA24 OK/SW-cl.81,GTP-binding nuclear protein Ran, 3.6.5.-, Androgen receptor-associated protein 24, GTPase Ran, Ras-like protein TC4, Ras-related nuclear protein, RAN, ARA24, OK/SW-cl.81

Human

WB,IHC,ELISA

WB 1:500-1:2000
IHC 1:50-1:300
ELISA 1:5000-1:20000

25kD

Rabbit

Recombinant Human RAN (Met1-Asp171).

Polyclonal

IgG

Purified by antigen affinity column.

0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.