The c-Myb protein, encoded by the MYB proto-oncogene, is a transcription factor critical for cellular proliferation, differentiation, and apoptosis, particularly in hematopoietic lineages and certain cancers. Its activity is tightly regulated by post-translational modifications, including phosphorylation, which modulates its DNA-binding capacity, protein stability, and interactions with co-regulators. Phosphorylation at Serine 11 (Ser11) is a key regulatory event linked to cell cycle progression and transcriptional activation. Studies suggest that this modification may influence c-Myb's ability to activate target genes involved in hematopoiesis, leukemogenesis, and other oncogenic processes.
The Phospho-c Myb (Ser11) antibody is a specialized tool designed to detect c-Myb specifically phosphorylated at Ser11. It is commonly used in techniques like Western blotting, immunofluorescence, or immunohistochemistry to study c-Myb activation dynamics in response to signaling pathways (e.g., MAPK/ERK) or cellular stressors. Researchers employ this antibody to explore how Ser11 phosphorylation impacts c-Myb’s role in normal development, tumorigenesis, or drug resistance. Validation typically includes testing in knockout models or phosphorylation-deficient mutants to ensure specificity. Understanding c-Myb regulation at Ser11 provides insights into disease mechanisms and potential therapeutic targets, particularly in hematologic malignancies where c-Myb dysregulation is prevalent.