Phospho-CREB (Ser133) antibodies are essential tools for studying the activation status of cAMP response element-binding protein (CREB), a transcription factor central to numerous cellular processes, including synaptic plasticity, memory formation, and cell survival. CREB becomes functionally active upon phosphorylation at serine 133 (Ser133), a modification that enables its interaction with transcriptional coactivators like CBP/p300. This phosphorylation event is primarily mediated by kinases such as protein kinase A (PKA), mitogen-activated protein kinase (MAPK), or calcium/calmodulin-dependent kinases (CaMKs), often in response to extracellular signals like hormones, growth factors, or neurotransmitters.
Phospho-specific antibodies targeting Ser133 allow researchers to detect and quantify the activated form of CREB in various experimental settings, including Western blotting, immunohistochemistry, and flow cytometry. These antibodies are particularly valuable in neuroscience, cancer biology, and metabolic research, where dysregulated CREB activity is linked to diseases like Alzheimer’s, cancer, and diabetes. For instance, elevated phospho-CREB levels are observed in certain tumors, correlating with enhanced cell proliferation and survival.
When using these antibodies, proper sample preparation is critical to preserve phosphorylation signals, as phosphatases in lysates can rapidly dephosphorylate CREB. Controls, such as unstimulated samples or kinase inhibitors, are recommended to validate specificity. Overall, phospho-CREB (Ser133) antibodies serve as indispensable probes for unraveling CREB-related signaling dynamics in health and disease.