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Caldesmon is an actin-binding protein that regulates actin cytoskeleton organization and assembly in smooth muscle and non-muscle cells.1,2 It is composed of an N-terminal myosin-binding domain, a central spacer region, and a C-terminal domain that contains binding sites for actin, as well as calmodulin and tropomyosin, and is subject to phosphorylation by a variety of kinases.1 Alternative splicing of the CALD1 pre-mRNA produces a heavy isoform, h-CaD, which is expressed by differentiated smooth muscle cells and localizes to actomyosin contractile structures, and a light isoform, l-CaD, which lacks the central spacer region and is expressed in non-muscle cells, where it localizes to podosomes and membrane ruffles.1,2 Caldesmon regulates the interaction between actin and myosin, influencing cell contractility and cytoskeletal remodeling in an isoform- and cell-dependent manner.2 It inhibits the activity of actomyosin ATPase, an effect that is enhanced by tropomyosin and reversed by Ca2+-calmodulin or phosphorylation. Increased caldesmon protein expression has been found in patients with metastatic oral squamous cell carcinoma (OSCC) and is associated with poor prognosis.3 Cayman's Caldesmon (C-Term) Rabbit Monoclonal Antibody (RM396) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Caldesmon and the regulation of cytoskeletal functions. Adv. Exp. Med. Biol. 644, 250-272 (2008).
2. Roles of caldesmon in cell motility and actin cytoskeleton remodeling. International Review of Cell and Molecular Biology 274, 1-51 (2009).
3. Caldesmon expression in metastatic and non-