The cytoskeleton is a structure that helps cells maintain their shape and internal organization and provides mechanical support enabling cells to perform vital functions like cell division and movement. The cytoskeleton consists of microtubules, intermediate filaments, and microfilaments. Tubulin is the protein component of microtubules. Heterodimers of α/β tubulin polymerize to from protofilaments. Thirteen protofilaments then assemble to form microtubules, which are hollow rod-like filaments. Microtubules are dynamic with tubulin dimers being added and removed at both ends of the filament. The end of the filament that grows the most rapidly is known as the plus end, whereas the other end of the filament is called the minus end. In cells, the minus end of microfilaments is anchored in microtubule organizing centres (MTOCs). The best studied MTOCs is the centrosome and is usually situated adjacent to the nucleus. Microtubules extend from the centrosome to the plasma membrane and provide the basic organisation of the cytoplasm and are involved in the intra-cellular transport of organelles. During cell division the centrosome forms a spindle that mediates the separation of chromosomes. There are several types of intermediate filaments composed of specific proteins that are expressed in different cell types. Intermediate filaments play a structural role providing mechanical strength to cells. Neurofilaments are intermediate filaments found in neurons. Desmin filaments are present in muscle cells and keratins are associated with epithelial cells. Vimentin is an intermediate filament found in a wide range of cells including fibroblasts, endothelial cells and leukocytes. Lamins are located in all cell types where they form a meshwork that reinforces the inner nuclear membrane. Intermediate filaments are formed from two polypeptides that wind around each other to form dimers with a coiled-coil structure. Dimers then associate into tetramers with a staggered anti-parallel structure. Tetramers subsequently associate end to end to form protofilaments and laterally to form filaments. Each intermediate filament comprises approximately eight protofilaments wound around each other in a rope-like structure. The main component of the cytoskeleton is actin. Actin exists as six isoforms: three α-actin isoforms (α-skeletal muscle, α-cardiac muscle and α-vascular), one β-isoform (β-cytoplasmic) and two γ-isoforms (γ-cytoplasmic and γ-smooth muscle). Actin monomers, globular [G] actin, polymerize to form filamentous [F] actin. Two F actin filaments then assemble to form a double helical structure. Similar to microtubules, actin filaments also have plus and minus ends, with more ATP-dependent growth occurring at the plus end. Actin filaments/microfilaments are organized into higher-order structures, forming bundles or networks. The assembly and disassembly of actin filaments, their crosslinking into bundles and networks and their association with other sub-cellular structures are regulated by actin-binding proteins. Actin filaments are abundant beneath the plasma membrane, where they form a network that provides mechanical support, determines cell shape, and enables movement of the cell surface, therefore facilitating cell migration, the engulfment of particles, and cell division. We offer a large range of cytoskeleton markers including GAPDH antibodies, Vimentin antibodies, HSP27 antibodies, and Desmin antibodies, as well as Tau antibodies which are neuron-specific. Our antibodies are tested for use in multiple applications and come in a range of different host species, clonalities, conjugates, and formulations.