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Ral Activation Assay Kit (ab212012) utilizes RalBP1 PBD Agarose beads to selectively isolate and pull-down the active form of Ral (RalA and RalB) from purified samples or endogenous lysates. Subsequently, the precipitated GTP-Ral is detected by western blot analysis using an anti-Ral A antibody, which detects the human, mouse, rat, chicken and dog protein.

Features: 1) non radioactive assay format; 2) fast results: 1 hour assay plus electrophoresis/blotting time; 3) includesCdc42 positive control; 4) pink colored agarose beads for easy identification during washing and aspiration steps.

Small GTP-binding proteins (or GTPases) are a family of proteins that serve as molecular regulators in signaling transduction pathways.

The Ral proteins (RalA and RalB) belong to the Ras superfamily. They share 85% identity with each other and 58% with the oncoproteins H-Ras, K-Ras and N-Ras. Both RalA and RalB are 24 kDa proteins that regulate a variety of biological response pathways including vesicle trafficking, oncogenesis, transcription regulation and cell morphology. Like other small GTPases, Ral regulates molecular events by cycling between an inactive GDP-bound form and an active GTP-bound form. In their active (GTP-bound) state, Ral A and Ral B bind specifically to the protein-binding domain (PBD) of RalBP1 to control downstream signaling cascades.

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RalA positive control (10 L of 293 cell lysate at 0.5 mg/mL) detected by immunoblot.

Ral activation assay. Lane 1: NIH 3T3 cell lysate loaded with GDP and incubated with RalBP1 PBD Agarose beads. Lane 2: NIH 3T3 cell lysate loaded with GTP S and incubated with RalBP1 PBD Agarose beads.

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