Rabbit Polyclonal MARCKS(phospho-Ser170) Antibody

The MARCKS (Myristoylated Alanine-Rich C-Kinase Substrate) protein is a prominent substrate for protein kinase C (PKC) and plays critical roles in cell signaling, membrane-cytoskeletal interactions, and cellular processes like secretion, migration, and proliferation. Phosphorylation at Serine 170 (Ser170) is a key regulatory mechanism controlling MARCKS function. Upon PKC activation, phosphorylation at Ser170 disrupts MARCKS' binding to actin and plasma membrane components, modulating its ability to crosslink actin filaments or sequester signaling molecules like phosphatidylinositol 4.5-bisphosphate (PIP2). This post-translational modification is implicated in diverse physiological and pathological contexts, including cancer metastasis, neuroinflammation, and synaptic plasticity. Antibodies specific to MARCKS phosphorylated at Ser170 (phospho-Ser170) are essential tools for studying PKC-MARCKS signaling dynamics. They enable detection of the active, phosphorylated form of MARCKS in techniques like Western blotting, immunofluorescence, or immunohistochemistry. Such antibodies help researchers explore spatiotemporal regulation of MARCKS activity in response to extracellular stimuli, disease states, or pharmacological interventions targeting PKC pathways. Validation often includes testing in phosphorylation-deficient mutants or PKC inhibitor-treated samples to confirm specificity. These antibodies are widely used in neuroscience, oncology, and immunology research to dissect mechanisms underlying cell motility, membrane trafficking, and disease progression.