Anti-RAPH1 / Ras-associated and pleckstrin homology domains-containing protein 1

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. The RAPH1 antibody targets Ras-associated and pleckstrin homology domains-containing protein 1, a membrane-associated adaptor encoded by the RAPH1 gene. Also known as lamellipodin, this protein coordinates actin cytoskeleton remodeling, cell migration, and adhesion through interactions with Ena/VASP and small GTPases. Ras-associated and pleckstrin homology domains-containing protein 1 acts as a link between membrane signaling and actin polymerization, facilitating lamellipodia formation at the leading edge of motile cells. The RAPH1 antibody enables specific detection of this regulatory molecule in studies of motility, morphogenesis, and cell polarity.Ras-associated and pleckstrin homology domains-containing protein 1 contains Ras-association and pleckstrin homology domains that mediate binding to activated Ras and phosphoinositides, respectively. These domains anchor RAPH1 to the plasma membrane where it recruits actin regulators such as Ena/VASP proteins to promote filament elongation. The RAPH1 antibody supports localization studies revealing how this scaffold integrates receptor-mediated signaling with actin dynamics. Its enrichment at lamellipodia and adhesion sites underscores its central role in coordinating directional migration.RAPH1 interacts with the small GTPase Rap1 to influence integrin activation and cell adhesion. By bridging signaling pathways that control cytoskeletal organization, it contributes to epithelial integrity, immune cell motility, and neuronal pathfinding. The RAPH1 antibody allows visualization of these processes, providing insight into mechanisms governing cell migration during wound healing and development. RAPH1 dysfunction can impair motility or lead to aberrant invasion in tumor cells.Lamellipodin has also been implicated in cancer progression and metastasis. Its overexpression enhances actin polymerization and invasive potential in various cancers including breast and colorectal carcinoma. The RAPH1 antibody supports analysis of these oncogenic roles by enabling quantification of protein levels in tumor tissues. Additionally, RAPH1 participates in mechanotransduction pathways by translating substrate stiffness into cytoskeletal rearrangement, linking extracellular cues to motility responses.The RAPH1 antibody performs effectively in western blotting, immunofluorescence, and immunohistochemistry, yielding distinct membrane and cytoplasmic staining consistent with lamellipodial localization. NSJ Bioreagents provides this antibody as a validated, high-specificity reagent suitable for cell biology and oncology research. By enabling detailed study of Ras-associated and pleckstrin homology domains-containing protein 1, the RAPH1 antibody advances understanding of cytoskeletal signaling, adhesion regulation, and directional migration in physiological and pathological contexts.