The Phospho-Rb2 p130 (Ser952) antibody is a specialized tool used to detect the phosphorylated form of the retinoblastoma-like protein p130 (RBL2) at serine residue 952. Rb2/p130. a member of the retinoblastoma tumor suppressor family (including Rb/p105. p107. and p130), plays a critical role in cell cycle regulation by interacting with E2F transcription factors to repress cell cycle progression, particularly in the G0/G1 phase. Phosphorylation of p130 at specific residues, such as Ser952. modulates its function by disrupting its binding to E2F, thereby releasing E2F-mediated transcriptional repression and allowing cell cycle entry. This phosphorylation event is typically mediated by cyclin-dependent kinases (CDKs) during cell cycle transitions, especially in response to mitogenic signals.
The antibody is widely used in cancer research to study aberrant cell cycle regulation, as dysregulation of p130 phosphorylation is implicated in tumorigenesis. It helps assess the activation status of p130 in various cellular contexts, including differentiation, senescence, and apoptosis. Researchers employ this antibody in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate cell cycle dynamics, therapeutic responses to CDK inhibitors, or correlations between p130 phosphorylation and disease progression. Its specificity for the phosphorylated Ser952 epitope makes it valuable for distinguishing active from inactive p130 in experimental models, contributing to understanding tumor suppressor mechanisms and developing targeted therapies.