Alpha Tubulin Antibodies

Background

Alpha Tubulin, as a major component protein of the cellular microtubule system, is widely present in the cytoplasm and cytoskeleton of eukaryotes. This protein forms a microtubule structure through polymerization, which not only maintains cell morphology but also participates in key physiological processes such as mitosis and intracellular substance transport. Because the dynamic assembly of microtubules plays a core role in the growth of neuronal axons, Alpha Tubulin has attracted much attention in the field of neural development. Its three-dimensional structure was first analyzed by electron crystallography in the 1980s, revealing the molecular mechanism of the GTP binding domain in the regulation of microtubule polymerization. As highly conserved cytoskeletal proteins, the research on their structure and function has greatly promoted breakthroughs in fields such as cell division, ciliary movement, and anti-cancer drug targets.

Structure Function Application Advantage Our Products

Structure of Alpha Tubulin

Alpha Tubulin is a conserved structural protein with a molecular weight of approximately 50 kDa, and its precise molecular weight varies slightly among different species.

Species	Human	Mouse	Yeast	Arabidopsis thaliana	Bovine
Molecular Weight (kDa)	50.1	49.9	49.8	49.7	50.0
Primary Structural Differences	There are multiple post-translational modification sites at the C-terminal tail	Highly homologous to the human sequence	Core structure domain highly conservative	Adapt to the unique microtubule functions of plants	As a commonly used experimental material, it has a stable structure

This protein is composed of approximately 450 amino acids, and its primary structure folds to form a hollow spherical core structure composed of alternating β -sheets and α -helices. This GTP-binding domain acts as a "molecular switch" to regulate the polymerization and depolymerization kinetics of tubulin dimers through the hydrolysis of GTP. Its functional activity is highly dependent on the heterodimer formed with β-tubulin, and this composite conformation provides the basic structural unit for microtubule assembly.

Fig. 1:Strategy for the selection of α-tubulin-specific αReps. Fig. 1 Strategy for the selection of α-tubulin-specific αReps.¹

Key structural properties of Alpha Tubulin:

Hollow globular GTPase domain composed of β-lamellar and α-helix
Exposed acidic C-terminal tail
Conservative GTP binding site
The heterodimer interface formed with β-Tubulin

Functions of Alpha Tubulin

The core function of Alpha Tubulin is to form cellular microtubules and regulate their dynamic assembly. In addition, it is also involved in a variety of key cellular activities, including intracellular transport and regulation of cell division.

Function	Description
Microtubule polymerization	With beta Tubulin heterologous dimers, longitudinal as basic unit assembly, forming hollow structure of microtubules.
Maintenance of cell morphology	By forming a cytoskeletal network, it provides mechanical support for cells and determines their morphology and polarity.
Mitotic regulation	Assemble to form a spindle, accurately capture and arrange chromosomes, and ensure their equal separation into daughter cells.
Intracellular transport	Provides tracks for motor proteins such as kinesin, dynein, and mediates the directed transport of vesicles and organelles.
Signal transduction	As a molecular platform, it participates in the transduction and regulation processes of multiple key signaling pathways such as Hedgehog and Hippo.

The growth of microtubules stems from the continuous addition of GTP-bound αβ -heterodimers at the end, while the hydrolysis of GTP triggers structural instability and contraction. This "dynamic instability" enables the microtubule network to rapidly reconstruct to adapt to changes in the cell cycle and external environment.

Applications of Alpha Tubulin and Alpha Tubulin Antibody in Literature

1. Iuzzolino, Angela, et al. "The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases." Cellular and Molecular Life Sciences 81.1 (2024): 193. https://doi.org/10.1007/s00018-024-05227-x

The article indicates that acetylation at the K40 site of α -tubulin can enhance the stability of microtubules. Its acetyltransferase ATAT1 plays a significant role in cell movement, mitosis and other processes, and is related to human diseases. Research on related inhibitors is also ongoing.

2. Diao, Lei, et al. "Cryo-EM of α-tubulin isotype-containing microtubules revealed a contracted structure of α4A/β2A microtubules: α4A/β2A microtubules display contracted lattices." Acta Biochimica et Biophysica Sinica 55.10 (2023): 1551. https://doi.org/10.3724/abbs.2023130

In this study, the microtubule structures composed of different α -tubulin isotypes (α1A, α1C, α4A) and β2A were resolved by cryo-electron microscopy. The results showed that the α4A/β2A microtubules contracted longitudinally between heterodimers, revealing for the first time that the α -tubulin isotype could determine the structural differences of microtubules, providing direct evidence for the "tubulin code" hypothesis.

3. Alonso, Victoria Lucia, et al. "Alpha-tubulin acetylation in Trypanosoma cruzi: a dynamic instability of microtubules is required for replication and cell cycle progression." Frontiers in Cellular and Infection Microbiology 11 (2021): 642271. https://doi.org/10.3389/fcimb.2021.642271

In this study, in Trypanosoma cruzii, the acetylation of the α -tubulin K40 site is crucial for maintaining the stability of the cytoskeleton. Research has found that its acetyltransferase TcATAT is located in the cytoskeleton and flagella. Its overexpression can disrupt cellular structures such as mitochondria, hinder the cell cycle process, and enhance the parasite's resistance to microtubule depolymerization drugs.

4. Campanacci, Valérie, et al. "Selection and characterization of artificial proteins targeting the tubulin α subunit." Structure 27.3 (2019): 497-506. https://doi.org/10.1016/j.str.2018.12.001

In this study, artificial proteins specifically binding to α -tubulin were screened out from the αRep library. These αRep can dose-dependent inhibit microtubule assembly and specifically block the growth of the negative end of microtubules by targeting the longitudinal interface of α -tubulin, providing a new tool for studying the dynamic mechanism of microtubules.

5. Ryan, Louise A., et al. "Fasciola hepatica expresses multiple α-and β-tubulin isotypes." Molecular and biochemical parasitology 159.1 (2008): 73-78. https://doi.org/10.1016/j.molbiopara.2008.02.001

The article indicates that five types of α -tubulin isotypes have been identified in liver fluke, and their amino acid sequence similarity ranges from 72% to 95%. Phylogenetic analysis revealed that two of the α -tubulin proteins were significantly different from those derived from other flukes.

Creative Biolabs: Alpha Tubulin Antibodies for Research

Creative Biolabs specializes in the production of high-quality Alpha Tubulin antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom Alpha Tubulin Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our Alpha Tubulin antibodies, custom preparations, or technical support, contact us at email.

Reference

Campanacci, Valérie, et al. "Selection and characterization of artificial proteins targeting the tubulin α subunit." Structure 27.3 (2019): 497-506. https://doi.org/10.1016/j.str.2018.12.001