β-Tubulin belongs to the subfamily of tubulin, which is the major building block of microtubules. β-tubulin has a molecular weight of 55kDa. β-Tubulin structure is characterized with core of two β-sheets enclosed by α-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 β-tubulin consists of seven isoforms (βI (class I), βII (class II), βIII (class III), βIVa (class IVa), βIVb (class IVb), βV (class V), and βVI (class VI)).
Immunogen
sarkosyl-resistant ribbons from Strongylocentrotus purpuratus (sea urchin) sperm axonemes.
Application
Monoclonal Anti-β-Tubulin antibody produced in mouse has been used in western blotting and fluorescence immunocytochemical staining.
Biochem/physiol Actions
Mutation in the gene leads to various neuronal migration disorders such as lissencephaly, pachygyria and polymicrogyria malformations. B2702 peptide binds to β-tubulin and inhibits NK cell cytotoxicity and it influences microtubule polymerization, which damages cytoskeleton organization and chaperone-like activity of tubulin. β-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).
The antibody recognizes the two major and one of the minor β‑tubulin isotypes of the free-living soil nematode C. elegans. It also binds to Sarkosyl-resistant ribbons from Strongylocentrotus purpuratus sperm axonemes, to neuronal axons of the larva of an ascidian (Ciona intestinalis) and to tubulin of chicken and mammals, cultured human fibroblasts, bovine and rat brain tissue. In C.elegans preparations, the antibody does not recognize tubulin that has been heat denatured in the presence of SDS and β-mercaptoethanol, though it is bound to tubulin separated on isoelectric focusing gels. It reacts with heat-denatured and reduced mammalian preparations in immunoblotting.
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Microtubules of the eukaryotic cytoskeleton are composed of a heterodimer of α- and β-tubulin. In addition to α-and β-tubulin, several other tubulins have been identified, bringing the number of distinct tubulin classes to seven.
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