Recombinant Human Tubulin alpha-1A chain (TUBA1A)

Code CSB-YP754656HU
MSDS
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Source Yeast
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Code CSB-EP754656HU
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Source E.coli
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Code CSB-EP754656HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP754656HU
MSDS
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Source Baculovirus
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Code CSB-MP754656HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
TUBA1A
Uniprot No.
Alternative Names
Alpha tubulin 3; Alpha-tubulin 3; B alpha 1; FLJ25113; LIS3; TBA1A_HUMAN; TUBA1A; TUBA3; Tubulin alpha 1a; Tubulin alpha 1A chain; Tubulin alpha 3; Tubulin alpha 3 chain; Tubulin alpha brain specific; Tubulin alpha-1A chain; Tubulin alpha-3 chain; Tubulin B alpha 1; Tubulin B-alpha-1
Species
Homo sapiens (Human)
Expression Region
1-451
Target Protein Sequence
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
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.
Gene References into Functions
  1. A de novo heterozygous c.320A>G [p.(His 107 Arg)] mutation in TUBA1A was identified in a patient with microcephaly, epileptic seizures, and severe developmental delay. PMID: 29109381
  2. Given that Spastin engages the MT in two places, we propose that severing occurs by forces exerted on the C-terminal tail of tubulin, which results in a conformational change in tubulin, which releases it from the polymer. PMID: 17389232
  3. Molecular docking studies revealed that 6f interacted and bound ef fi ciently with the colchicine-binding site of tubulin. In addition, 6f treatment induced G2/M cell cycle arrest dose-dependently and subsequently induced cell apoptosis PMID: 28440465
  4. induced pluripotent stem cells (iPSCs) from the umbilical cord and peripheral blood of two lissencephaly patients with different clinical severities carrying alpha tubulin (TUBA1A) missense mutations, were generated. PMID: 27431206
  5. Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin acetylation in breast cancer. PMID: 27228351
  6. Results show that Tuba1a plays an essential, noncompensated role in neuronal saltatory migration in vivo and highlight the importance of microtubule flexibility in nucleus-centrosome coupling and neuronal-branching regulation during neuronal migration. PMID: 28687665
  7. data suggest that the TUBA1A mutations disrupting lateral interactions have pronounced dominant-negative effects on microtubule dynamics that are associated with the severe end of the lissencephaly spectrum PMID: 26493046
  8. Data show that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability. PMID: 26165356
  9. Data show that plasma membrane Ca(2+)-ATPase (PMCA) was associated with tubulin in normotensive and hypertensive erythrocytes. PMID: 26307527
  10. Studies indicate that alpha-tubulin acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). PMID: 26227334
  11. Data from studies using peptide fragment of alpha-tubulin (residues 31-49) suggest that Ser38 is crucial for substrate recognition by alpha-tubulin acetylase 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 result in significant changes in kinesin-1's landing rate or motility parameters. PMID: 24940781
  13. These results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). PMID: 24914767
  14. This study show all foetuses with lissencephaly and cerebellar hypoplasia carried distinct TUBA1A mutations. PMID: 25059107
  15. These findings call attention to PKC-mediated phosphorylation of alpha-tubulin as a novel mechanism for controlling the dynamics of microtubules that result in cell movement. PMID: 24574051
  16. case provides new insight into the wide spectrum of disease phenotypes associated with TUBA1A mutation PMID: 23528852
  17. The present study confirms that mutations in tubulin genes are responsible for complex brain malformation. PMID: 24392928
  18. Studies suggest that tubulin-interactive agents have the potential to play a significant role in the fight against cancer. PMID: 23818224
  19. Missense mutations in TUBA1A were found in 3 patients with polymicrogyria. PMID: 22948023
  20. We described the clinical course and pathological findings in a child with TUBA1A mutation PMID: 22633752
  21. TUBA1A and TUBB2B coding regions have been sequenced that are associated with cortical malformations. PMID: 23361065
  22. Data show that Na(+),K(+)-ATPase activity was >50% lower and membrane-associated tubulin content was >200% higher in erythrocyte membranes from diabetic patients. PMID: 22565168
  23. study describes a 14-month-old girl with TUBA1A mutation-associated lissencephaly, and summarize the clinical and neuroradiologic findings of 19 cases in the literature PMID: 22264709
  24. Alpha2B-adrenergic receptor interaction with tubulin controls its transport from the endoplasmic reticulum to the cell surface PMID: 21357695
  25. The expression of alpha-tubulin and MDR1 may play an important role in the development and progression of human non-small cell lung carcinoma. PMID: 20510079
  26. We report a mutation in TUBA1A as a cause of polymicrogyria. So far, all mutations in TUBA1A have occurred de novo, resulting in isolated cases. This article describes familial recurrence of TUBA1A mutations due to somatic mosaicism in a parent. PMID: 21403111
  27. Data show that IAV-infected cells contain elevated level of AcTub and alpha-tubulin. PMID: 21094644
  28. Mutations in TUBA1A result in defects in the tubulin folding and heterodimer assembly. PMID: 20603323
  29. LIS-associated mutations of TUBA1A operate via diverse mechanisms that include disruption of binding sites for microtubule-associated proteins. PMID: 20466733
  30. the dipole moments of each tubulin isotype may influence their functional characteristics within the cell, resulting in differences for MT assembly kinetics and stability PMID: 16941085
  31. Mutations in alpha-tubulin in mice and humans that affect neuronal migration result in abnormal lamination of brain structures with associated behavioral deficits. PMID: 17218254
  32. Retrospective examination of MR images suggests that patients with TUBA1A mutations share not only cortical dysgenesis, but also cerebellar, hippocampal, corpus callosum, and brainstem abnormalities PMID: 17584854
  33. Increased expression of tubulin alpha is associated with pulmonary sclerosing hemangioma PMID: 17914564
  34. The diminished production of TUBA1A tubulin in R264C individuals is consistent with haploinsufficiency as a cause of the disease phenotype. PMID: 18199681
  35. the TUBA1A phenotype is distinct from LIS1, DCX, RELN and ARX lissencephalies. Compared with the phenotypes of children mutated for TUBA1A, these prenatally diagnosed fetal cases occur at the severe end of the TUBA1A lissencephaly spectrum. PMID: 18669490
  36. Missense mutations within the TUBA1A gene are associated with specific abnormalities in lissencephaly. PMID: 18728072
  37. mutation analysis in the TUBA1A gene in 46 patients with classical lissencephaly. PMID: 18954413
  38. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953

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Involvement in disease
Lissencephaly 3 (LIS3)
Subcellular Location
Cytoplasm, cytoskeleton.
Protein Families
Tubulin family
Tissue Specificity
Expressed at a high level in fetal brain.
Database Links

HGNC: 20766

OMIM: 602529

KEGG: hsa:7846

STRING: 9606.ENSP00000301071

UniGene: Hs.654422

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