Anti-Tubulin alpha Picoband® Antibody (monoclonal, 7B12) Fluoro647 Conjugated

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. Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to the mouse and rat Tuba1 genes. Northern blot studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q. Mutations in this gene cause lissencephaly type 3 (LIS3) - a neurological condition characterized by microcephaly, intellectual disability, and early-onset epilepsy caused by defective neuronal migration. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

SUMO-activating enzyme subunit 2; Anthracycline-associated resistance ARX; Ubiquitin-like 1-activating enzyme E1B; Ubiquitin-like modifier-activating enzyme 2; UBA2; SAE2, UBLE1B; HRIHFB2115

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.

1. Aiken, J., Moore, J. K., Bates, E. A. TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity. Hum. Molec. Genet. 28: 1227-1243, 2019. 2. Bahi-Buisson, N., Poirier, K., Boddaert, N., Saillour, Y., Castelnau, L., Philip, N., Buyse, G., Villard, L., Joriot, S., Marret, S., Bourgeois, M., Van Esch, H., Lagae, L., Amiel, J., Hertz-Pannier, L., Roubertie, A., Rivier, F., Pinard, J. M., Beldjord, C., Chelly, J. Refinement of cortical dysgeneses spectrum associated with TUBA1A mutations. J. Med. Genet. 45: 647-653, 2008. 3. Cowan, N. J., Dobner, P. R., Fuchs, E. V., Cleveland, D. W. Expression of human alpha-tubulin genes: interspecies conservation of 3-prime untranslated regions. Molec. Cell. Biol. 3: 1738-1745, 1983.