Recombinant Human Tubulin alpha-1A chain (TUBA1A)

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Tubulin is the primary component 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.

1. A de novo heterozygous c.320A>G [p.(His107Arg)] mutation in TUBA1A was identified in a patient presenting with microcephaly, epileptic seizures, and severe developmental delay. PMID: 29109381
2. Spastin's interaction with the microtubule at two points suggests that severing occurs through forces exerted on the C-terminal tail of tubulin, inducing a conformational change that releases it from the polymer. PMID: 17389232
3. Molecular docking studies indicated efficient interaction and binding of compound 6f with the colchicine-binding site of tubulin. 6f treatment dose-dependently induced G2/M cell cycle arrest, followed by apoptosis. PMID: 28440465
4. Induced pluripotent stem cells (iPSCs) were generated from umbilical cord and peripheral blood samples of two lissencephaly patients with varying clinical severities, both carrying alpha-tubulin (TUBA1A) missense mutations. PMID: 27431206
5. The long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by reducing alpha-tubulin acetylation in breast cancer. PMID: 27228351
6. Tuba1a plays a crucial, non-compensated role in neuronal saltatory migration *in vivo*, highlighting the importance of microtubule flexibility in nucleus-centrosome coupling and neuronal branching regulation during neuronal migration. PMID: 28687665
7. TUBA1A mutations disrupting lateral interactions exhibit pronounced dominant-negative effects on microtubule dynamics, correlating with severe lissencephaly. PMID: 26493046
8. Tubulin phosphorylation and acetylation are key regulators of microtubule assembly and stability. PMID: 26165356
9. Plasma membrane Ca(2+)-ATPase (PMCA) associates with tubulin in both normotensive and hypertensive erythrocytes. PMID: 26307527
10. Alpha-tubulin acetylation and microtubule levels are primarily governed by the opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). PMID: 26227334
11. Studies using an alpha-tubulin peptide fragment (residues 31-49) indicate that Ser38 is crucial for substrate recognition by alpha-tubulin acetyltransferase 1 (ATAT1); Asp39, Ile42, the glycine stretch (residues 43-45), and Asp46 are also involved. PMID: 25602620
12. Lysine 40 acetylation of alpha-tubulin does not significantly alter kinesin-1's landing rate or motility parameters. PMID: 24940781
13. SelP interacts with tubulin alpha 1a (TUBA1A). PMID: 24914767
14. All fetuses with lissencephaly and cerebellar hypoplasia exhibited distinct TUBA1A mutations. PMID: 25059107
15. PKC-mediated phosphorylation of alpha-tubulin represents a novel mechanism for controlling microtubule dynamics and subsequent cell movement. PMID: 24574051
16. This case study provides insights into the broad spectrum of phenotypes associated with TUBA1A mutations. PMID: 23528852
17. Mutations in tubulin genes are implicated in complex brain malformations. PMID: 24392928
18. Tubulin-interactive agents hold potential as significant tools in cancer treatment. PMID: 23818224
19. Missense mutations in TUBA1A were identified in three patients with polymicrogyria. PMID: 22948023
20. This report details the clinical course and pathological findings in a child with a TUBA1A mutation, summarizing findings from 19 cases in the literature. PMID: 22633752
21. Sequencing of the TUBA1A and TUBB2B coding regions revealed associations with cortical malformations. PMID: 23361065
22. Na(+),K(+)-ATPase activity was >50% lower, and membrane-associated tubulin content was >200% higher in erythrocyte membranes from diabetic patients. PMID: 22565168
23. This study describes a 14-month-old girl with TUBA1A mutation-associated lissencephaly, summarizing clinical and neuroradiologic findings from 19 cases reported in the literature. PMID: 22264709
24. Alpha2B-adrenergic receptor interaction with tubulin regulates its transport from the endoplasmic reticulum to the cell surface. PMID: 21357695
25. Alpha-tubulin and MDR1 expression may play a significant role in the development and progression of human non-small cell lung carcinoma. PMID: 20510079
26. This report details a TUBA1A mutation as a cause of polymicrogyria, noting the familial recurrence of TUBA1A mutations due to somatic mosaicism in a parent. PMID: 21403111
27. IAV-infected cells exhibit elevated levels of AcTub and alpha-tubulin. PMID: 21094644
28. TUBA1A mutations lead to defects in tubulin folding and heterodimer assembly. PMID: 20603323
29. Lissencephaly-associated TUBA1A mutations disrupt binding sites for microtubule-associated proteins. PMID: 20466733
30. The dipole moments of individual tubulin isotypes may influence their cellular function, impacting microtubule assembly kinetics and stability. PMID: 16941085
31. Alpha-tubulin mutations in mice and humans affecting neuronal migration result in abnormal brain lamination and associated behavioral deficits. PMID: 17218254
32. Retrospective analysis of MRI images suggests that patients with TUBA1A mutations exhibit cortical dysgenesis and abnormalities in the cerebellum, hippocampus, corpus callosum, and brainstem. PMID: 17584854
33. Increased tubulin alpha expression is associated with pulmonary sclerosing hemangioma. PMID: 17914564
34. Diminished TUBA1A tubulin production in R264C individuals is consistent with haploinsufficiency as a disease mechanism. PMID: 18199681
35. The TUBA1A phenotype differs from LIS1, DCX, RELN, and ARX lissencephalies. Prenatally diagnosed cases represent the severe end of the TUBA1A lissencephaly spectrum. PMID: 18669490
36. Missense mutations within the TUBA1A gene are associated with specific lissencephaly abnormalities. PMID: 18728072
37. Mutation analysis of the TUBA1A gene was performed in 46 patients with classical lissencephaly. PMID: 18954413
38. Differential expression of this protein was observed in Wernicke's Area of patients with schizophrenia. PMID: 19405953

HGNC: 20766

OMIM: 602529

KEGG: hsa:7846

STRING: 9606.ENSP00000301071

UniGene: Hs.654422