SpecificityAb11311 recognizes the two major beta tubulin isotypes and one of the minor beta-tubulin isotypes of the free-living soil nematode Caenorhabditis elegans.
It also binds to Sarkosyl-resistant ribbons from Strongylocentrotus purpuratus (sea urchin) sperm axonemes, to neuronal axons of the larva of Ciona intestinalis (ascidian), and to tubulin of chicken and mammals (e.g., 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 beta-mercaptoethanol, though it is bound to tubulin separated on isoelectric focusing gels, and found reactive with heat-denatured and reduced mammalian preparations in immunoblotting.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution. PubMed: 20663883
Use at an assay dependent dilution.
Use at an assay dependent dilution. Predicted molecular weight: 50 kDa.
FunctionTubulin 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.
Tissue specificityUbiquitously expressed with highest levels in spleen, thymus and immature brain.
Involvement in diseaseCortical dysplasia, complex, with other brain malformations 6 Skin creases, congenital symmetric circumferential, 1
Sequence similaritiesBelongs to the tubulin family.
DomainThe highly acidic C-terminal region may bind cations such as calcium.
Post-translational modificationsSome glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear. Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.
Immunocytochemistry/ Immunofluorescence - Anti-beta Tubulin antibody [2-28-33] (ab11311)Image from Jiang H et al, J Biol Chem. 2010 Oct 8;285(41):31634-46. Epub 2010 Jul 27, Fig 8. DOI 10.1074/jbc.M110.128645 October 8, 2010 The Journal of Biological Chemistry, 285, 31634-31646.
ab11311 staining beta tubulin in primary human keratinocytes by Immunocytochemistry/ Immunofluorescence. Cells treated with 0.1% DMSO for 18 hours.
References for Anti-beta Tubulin antibody [2-28-33] (ab11311)
This product has been referenced in:
Scharadin TM et al. TIG3 Tumor Suppressor-Dependent Organelle Redistribution and Apoptosis in Skin Cancer Cells. PLoS One6:e23230 (2011).
Read more (PubMed: 21858038) »
Jiang H et al. Type I transglutaminase accumulation in the endoplasmic reticulum may be an underlying cause of autosomal recessive congenital ichthyosis. J Biol Chem285:31634-46 (2010).
Read more (PubMed: 20663883) »