Anti-RALGAPB / Ral GTPase-activating protein subunit beta

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. RALGAPB antibody detects Ral GTPase-activating protein subunit beta, a large scaffolding component of the RalGAP complex that inactivates small GTPases RALA and RALB. The RalGAP complex consists of catalytic (RALGAPA1 or RALGAPA2) and regulatory (RALGAPB) subunits and serves as a negative regulator of Ral signaling, which is involved in membrane trafficking, cell migration, and tumorigenesis. The RALGAPB antibody is an essential reagent for exploring Ral-mediated signaling pathways and understanding their impact on oncogenic transformation and vesicular transport.RALGAPB is encoded by the RALGAPB gene located on human chromosome 20q13.33. The protein is cytoplasmic and interacts with Ral GTPases to stimulate their intrinsic GTP hydrolysis activity, thereby switching them from active (GTP-bound) to inactive (GDP-bound) states. Through this action, RALGAPB contributes to regulation of endocytosis, exocytosis, and actin cytoskeleton dynamics. It also links Ral signaling to insulin-stimulated GLUT4 vesicle trafficking in metabolic tissues.The RALGAPB antibody is widely used to detect the 185-200 kDa protein in western blot and to visualize cytoplasmic localization in immunofluorescence. RALGAPB forms a heterodimer with RALGAPA1 or RALGAPA2, and the resulting complex controls Ral-dependent regulation of mTOR signaling, autophagy, and vesicle movement. Studies have implicated RALGAPB in insulin sensitivity, as well as in cancer progression where Ral signaling is hyperactivated. Loss or mutation of RALGAPB leads to sustained Ral activity, promoting cellular proliferation and migration.Functional studies using this antibody have connected RALGAPB to the modulation of cell junction dynamics and receptor trafficking. It is also implicated in neuronal vesicle regulation and autophagosome maturation. NSJ Bioreagents offers a validated RALGAPB antibody optimized for western blot, immunoprecipitation, and immunofluorescence, enabling researchers to examine its role in signaling, vesicular transport, and metabolic regulation.