Bok (Bcl-2-related ovarian killer) is a member of the Bcl-2 protein family, which regulates apoptosis by modulating mitochondrial outer membrane permeabilization. Initially identified in ovarian tissue, Bok shares structural homology with pro-apoptotic family members like Bax and Bak, containing conserved BH (Bcl-2 homology) domains. However, its precise role remains debated. While some studies suggest Bok promotes apoptosis under specific conditions (e.g., DNA damage), others indicate it may paradoxically inhibit apoptosis or function independently of classical Bcl-2 pathways. Bok is highly expressed in reproductive tissues, the brain, and certain cancers, implicating it in tissue homeostasis and disease.
Bok antibodies are essential tools for detecting and studying Bok's expression, localization, and interactions. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence. Due to Bok's structural similarities to other Bcl-2 proteins, antibody specificity is critical to avoid cross-reactivity. Researchers often validate Bok antibodies using knockout cell lines or tissues to confirm target specificity. Commercial antibodies vary in host species, clonality (monoclonal/polyclonal), and epitope recognition, necessitating careful selection based on experimental needs.
Current research focuses on clarifying Bok's context-dependent functions, particularly its interplay with endoplasmic reticulum stress, cancer progression, and reproductive health. Reliable Bok antibodies remain pivotal in uncovering its biological and pathological significance.