Cullin2 antibody is a crucial tool in studying the Cullin2 protein, a scaffold component of the Cullin-RING E3 ubiquitin ligase (CRL) complexes. Cullin2. part of the Cullin protein family, forms the CRL2 complex by binding to Rbx1 (RING box protein 1) and Elongin B/C adaptors. This complex facilitates substrate recognition and polyubiquitination, targeting proteins for proteasomal degradation. Cullin2 is notably involved in regulating hypoxia-inducible factor (HIF)-α by interacting with the Von Hippel-Lindau (VHL) tumor suppressor protein, a key mechanism in oxygen-sensing pathways. Dysregulation of Cullin2 is linked to cancer, developmental disorders, and VHL disease.
Cullin2 antibodies are widely used in Western blotting, immunoprecipitation, and immunohistochemistry to detect protein expression, localization, and interactions in cellular and tissue samples. They aid in investigating Cullin2's role in cell cycle control, DNA damage response, and tumorigenesis. Researchers also utilize these antibodies to explore therapeutic strategies targeting CRL2 complexes, particularly in cancers with VHL mutations or HIF pathway activation. Commercial Cullin2 antibodies are typically raised against specific epitopes (e.g., N-terminal or C-terminal regions) and validated for cross-reactivity across species like human, mouse, and rat. Proper controls are essential due to potential cross-reactivity with other Cullin family members.