ß-Tubulin belongs to the subfamily of tubulin, which is the major building block of microtubules. ß-Tubulin has a molecular weight of 55kDa. ß-Tubulin structure is characterized with core of two ß-sheets enclosed by a-helices. It also contains an N-terminal domain with the guanine nucleotide-binding region, an intermediate domain with taxol-binding site, and a C-terminal domain that contains the binding surface for molecular motor proteins. Human ß-tubulin consists of seven isoforms (ßI (class I), ßI (class II), ßIII (class III), ßIVa (class IVa), ßIVb (class IVb), ßV (class V), and ßVI (class VI)).
Synonyms: Monoclonal Anti-beta-Tubulin
Storage: -20C
Application: Monoclonal Anti-ß-Tubulin antibody produced in mouse has been used in western blotting.
Biochem Physiol Actions: Mutation in the gene leads to various neuronal migration disorders such as lissencephaly, pachygyria and polymicrogyria malformations. B2702 peptide binds to ß-tubulin and inhibits NK cell cytotoxicity and it influences microtubule polymerization, which damages cytoskeleton organization and chaperone-like activity of tubulin. ß-1 tubulin also known as class VI or TUBB1, plays a vital role in platelet production, and is considered to be a potential biomarker candidate for immune thrombocytopenia (ITP).