Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. Microtubules function in many essential cellular processes, including mitosis. Tubulin-binding drugs kill cancerous cells by inhibiting microtubule dynamics, which are required for DNA segregation and therefore cell division. In eukaryotes there are six members of the tubulin superfamily, although not all are present in all species (see below). Both α and β tubulins have a mass of around 50 kDa and are thus in a similar range compared to actin with 42 kDa. In contrast, tubulin polymers (microtubules) tend to be much bigger than actin filaments due to their cylindrical nature.
Tubulin β Polyclonal Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. This antibody has been tested with ELISA, IF, IHC-p, WB. And Abbkine suggested starting dilutions are as follows: WB: 1:500-1:2000, IHC-p: 1:100-1:300, IF: 1:200-1:1000, ELISA: 1:5000.
All drugs that are known to bind to human tubulin bind to β-tubulin. These include paclitaxel, colchicine, and the vinca alkaloids, each of which have a distinct binding site on β-tubulin. Class III β-tubulin is a microtubule element expressed exclusively in neurons, and is a popular identifier specific for neurons in nervous tissue. It binds colchicine much more slowly than other isotypes of β-tubulin. We make experiments with this Antibody. The results of the experiment is satisfactory.