Recombinant Human beta I Tubulin protein (ab164310)

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.

Defects in TUBB1 are a cause of macrothrombocytopenia autosomal dominant TUBB1-related (MAD-TUBB1) [MIM:613112]. It is a congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets.

Belongs to the tubulin family.

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules.

Cytoplasm > cytoskeleton.