Rabbit Polyclonal MARCKS(Phospho-Ser162) Antibody

The MARCKS (Myristoylated Alanine-Rich C-Kinase Substrate) protein is a key intracellular substrate for protein kinase C (PKC), playing critical roles in cell signaling, cytoskeletal dynamics, and membrane-cytoskeleton interactions. Phosphorylation at Serine 162 (Ser162) is a major regulatory mechanism for MARCKS, triggered by PKC activation in response to extracellular signals like growth factors or neurotransmitters. This post-translational modification reduces MARCKS' affinity for the plasma membrane, releasing it into the cytoplasm and modulating its ability to crosslink actin filaments or sequester signaling molecules (e.g., PIP2). The MARCKS (Phospho-Ser162) antibody specifically detects this phosphorylated form, serving as a valuable tool to study PKC-mediated signaling pathways. Researchers use this antibody in techniques like Western blotting, immunofluorescence, or flow cytometry to investigate cellular processes such as cell adhesion, migration, secretion, and inflammatory responses. Dysregulation of MARCKS phosphorylation has been implicated in cancer metastasis, neurological disorders, and immune dysfunctions, making this antibody relevant for both basic research and translational studies targeting PKC-related diseases. Its specificity for the activated (phosphorylated) state allows precise tracking of dynamic cellular responses to stimuli.