Monoclonal Anti- β-Tubulin Antibody

Catalog# BTL1038

Lot # Check on the product label

Size 100μg

Isotype IgG1

Host Mouse

Reactivity

Human, mouse, rat, C.elegans, Fruit fly, goat, rabbit, chicken

Product Form Liquid (1mg/ml)

Immunogen 

Human β-Tubulin protein with full length.

Recommend Application

Western Blot (1:1000-10000)

Immunofluorescence, IF (1:200-1000)

Immunohistochemistry, IHC (1:200-1000)

Other applications have not been tested.

The optimal dilutions should be determined by end user.

Storage Buffer

In PBS (pH7.4), 50% Glycerol and 0.02% Sodium Azide.

Storage Instruction 

Store at -20°C for 1 year.

Avoid repeated freeze and thaw cycles.

Background

Tubulin is one of several members of a small family of globular proteins. The most common members of the tubulin family are α-tubulin and β-tubulin, the proteins that make up microtubules. Each has a molecular weight of approximately 55 kiloDaltons. Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8. Mutant huntingtin, disrupted intracellular transport and insulin secretion by direct interference with microtubular beta-tubulin. Mutant huntingtin impaired glucose-stimulated insulin secretion in insulin-producing beta cells, without altering stored levels of insulin. Smith et al. (2009) proposed a novel pathogenetic process by which mutant huntingtin may disrupt hormone exocytosis from beta cells and possibly impair vesicular transport in any cell that expresses the pathogenic protein.

Reference

1. Williams RC Jr, Shah C, Sackett D (November 1999). "Separation of tubulin isoforms by isoelectric focusing in immobilized pH gradient gels". Anal Biochem 275 (2): 265–7.

2. Smith, R., Bacos, K., Fedele, V., Soulet, D., Walz, H. A., Obermuller, S., Lindqvist, A., Bjorkqvist, M., Klein, P., Onnerfjord, P., Brundin, P., Mulder, H., Li, J.-Y. Mutant huntingtin interacts with beta-tubulin and disrupts vesicular transport and insulin secretion. Hum. Molec. Genet. 18: 3942-3954, 2009.