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|Reactivity||Human Mouse Rat|
|Tested applications||WB IHC|
|Recommended Dilution||WB 1:500 - 1:2000 IHC 1:50 - 1:200|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human RALBP1|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
The RalA binding protein 1 (RalBP1 or RLIP76) was originally identified as a GTP-RalA associated protein that acted as a downstream RalA effector in regulating Ral-Ras signaling (1). RalBP1 interacts with RalA and the endocytosis protein REPS2 (POB1) through its carboxy-terminal Ral binding domain. RalBP1 has an intrinsic GTPase activating function and interacts with Cdc42 through its centrally located Rho-GAP domain (1-3). A protein complex containing RalBP1/POB1/RalA regulates endocytosis of membrane receptors (4). RalBP1 also functions as a non-ABC transporter that catalyzes the ATP-dependent transport of numerous xenobiotics, including glutathione conjugates and some chemotherapeutic agents. RalBP1 transporter activity may play an important role in detoxification, drug resistance and the stress response (5-7). Increased expression of RalBP1 protein is associated with some forms of cancer and regression of cancer xenografts results from RalBP1 inhibition (8,9). Evidence to date suggests that RalBP1 may be a promising therapeutic target for cancer therapy.