Calmodulin (CaM) is a highly conserved, multifunctional Ca²⁺-binding protein that regulates a wide range of cellular processes, including signal transduction, enzyme activity, ion transport, and cytoskeletal organization. It functions by binding Ca²⁺ ions through its four EF-hand motifs, inducing conformational changes that enable interactions with target proteins such as kinases, phosphatases, and ion channels. Due to its central role in calcium-mediated signaling, Calmodulin is ubiquitously expressed in eukaryotic cells and is critical for processes like neurotransmission, muscle contraction, and immune response.
Calmodulin antibodies are essential tools for studying its expression, localization, and function in biological systems. These antibodies are typically generated using immunogenic peptides or recombinant Calmodulin proteins, with common hosts including rabbits, mice, or goats. They enable detection via techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and ELISA. Specific antibodies may distinguish between apo-CaM (Ca²⁺-free) and Ca²⁺-bound conformations or post-translationally modified forms, aiding research into calcium signaling dynamics.
Applications span neuroscience, cardiology, and cancer research, particularly in pathologies linked to Calmodulin dysregulation, such as neurodegenerative diseases, cardiac arrhythmias, and tumor progression. Validation of Calmodulin antibodies requires attention to cross-reactivity due to its homology across species and structural similarities with related EF-hand proteins.