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     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P08677(RASSF8 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

The RASSF8 antibody is a crucial tool for studying the Ras association domain family member 8 (RASSF8), a protein implicated in cellular adhesion, signaling, and tumor suppression. RASSF8 belongs to the RASSF family, which interacts with Ras GTPases to regulate pathways controlling cell proliferation, apoptosis, and cytoskeletal organization. Structurally, RASSF8 contains a conserved Ras-association (RA) domain and a coiled-coil domain, enabling interactions with membrane-associated proteins and cytoskeletal components. It localizes to cell-cell junctions and plays roles in maintaining epithelial integrity, cell migration, and polarity. Dysregulation of RASSF8 has been linked to cancers, including lung and colorectal malignancies, where its downregulation may promote metastasis.

The RASSF8 antibody, typically generated in rabbits or mice using immunogenic peptide sequences, allows detection and quantification of endogenous RASSF8 via techniques like Western blotting, immunofluorescence, and immunohistochemistry. Its specificity is validated using knockout controls or siRNA-mediated silencing to confirm minimal cross-reactivity with other RASSF members. Researchers employ this antibody to explore RASSF8's involvement in Hippo and MAPK signaling pathways, its tumor-suppressive functions, and its interplay with adherens junction proteins like E-cadherin. By enabling spatial and temporal analysis of RASSF8 expression, the antibody aids in elucidating its role in developmental biology, tissue homeostasis, and cancer progression, with potential applications in diagnostic or therapeutic biomarker discovery.