RALBP1 (RALA Binding Protein 1), also known as RLIP76 or RIP1. is a multifunctional protein involved in cellular processes such as endocytosis, oxidative stress response, and drug resistance. It acts as a GTPase-activating protein (GAP) for RalA and RalB, small GTPases in the Ras superfamily, regulating vesicular trafficking and signal transduction. RALBP1 also functions as an ATP-dependent transporter, mediating the efflux of glutathione-conjugated electrophiles (GS-E), contributing to detoxification and chemoresistance in cancer cells. Its role in stress response links it to pathways like MAPK/ERK and PI3K/AKT, impacting cell survival and apoptosis.
RALBP1 antibodies are essential tools for studying its expression, localization, and interactions in various contexts. These antibodies enable detection via Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF), helping researchers explore RALBP1's overexpression in cancers (e.g., lung, prostate, ovarian) and its association with aggressive tumor behavior and poor prognosis. Additionally, they aid in investigating RALBP1's involvement in neurodegenerative diseases, where oxidative stress mechanisms are implicated. Commercially available RALBP1 antibodies are typically raised in hosts like rabbit or mouse, targeting specific epitopes (e.g., N-terminal or C-terminal regions), and validated for cross-reactivity in human, mouse, or rat samples. Their applications extend to functional studies, such as siRNA knockdown validation or assessing therapeutic targeting in drug-resistant malignancies.