Tubulin Alpha antibody | YOL1/34
Rat anti tubulin alpha antibody, clone YOL1/34 (MCA78G) used as a loading control for the detection of tubulin-α in Candida albicans lysates by western blotting.
Image caption:
Staurosporine induces filamentation independent of Nrg1 degradation. (A) Staurosporine-induced filamentation is not accompanied by Nrg1 protein degradation. SN95 wild-type cells expressing native levels of HA-tagged Nrg1 were grown in YPD plus 10% serum at 37°C, YPD plus 200 mM hydroxyurea (HU) at 30°C, or YPD plus 0.5 μg/ml staurosporine at 30°C for 5 or 65 min. Total proteins were resolved by SDS-PAGE gel, and the blot was hybridized with anti-HA to detect Nrg1 and anti-tubulin to monitor tubulin as a loading control. (B) Staurosporine induces germ tube formation at different kinetics from serum and hydroxyurea. Cells were imaged by DIC microscopy. The scale bar indicates 10 μm.
From: Xie JL, O'Meara TR, Polvi EJ, Robbins N, Cowen LE.
Staurosporine Induces Filamentation in the Human Fungal Pathogen Candida albicans via Signaling through Cyr1 and Protein Kinase A.
mSphere. 2017 Mar 1;2(2). pii: e00056-17. eCollection 2017 Mar-Apr.
Rat anti tubulin alpha antibody, clone YOL1/34 (MCA78G) used for the illustration of mitotic spindles in wild type and Bsg25D mutant Drosophila embryos by immunofluorescence.
Image caption:
Detail from: Bsg25D mutant embryos have a reduced hatching rate and exhibit mitotic defects.
Anti-α-tubulin, anti-γ-tubulin immunostaining and DAPI staining of a wild-type embryo showing mitotic spindles. (G) Example of embryo graded as having severe mitotic defects. Two images of the same embryo showing two tripolar mitotic divisions (arrows) with γ-tubulin attached to mitotic spindle. In all images scale bar=50μm.
From: Kowanda M, Bergalet J, Wieczorek M, Brouhard G, Lécuyer É, Lasko P.
Loss of function of the Drosophila Ninein-related centrosomal protein Bsg25D causes mitotic defects and impairs embryonic development.
Biol Open. 2016 Aug 15;5(8):1040-51.
Rat anti tubulin-α antibody, clone YOL1/34 (MCA78G) used for the detection of tubulin-α in HeLa cells by immunofluorescence.
Image caption:
Role of the phosphorylation of ATF7 in G2/M progression. (A) Parental HeLa S3/TR, HeLa S3/TR/ATF7-wt (cl.2), or HeLa S3/TR/ATF7-TA (cl.1) cells were synchronized using DTB and released into thymidine-free medium containing 1 µg/ml Dox for 12 h. Whole cell lysates were analyzed by WB. Full-length blots are presented in S12A Fig. (B) HeLa S3/TR/ATF7-wt (cl.2) (upper panels) or HeLa S3/TR/ATF7-TA (cl.1) cells (lower panels) were synchronized using single-thymidine block and released into thymidine-free medium containing 1 µg/ml Dox for 11 h. Cells were triply stained with anti-ATF7[SAB2500131] and anti-α-tubulin antibodies and PI (for DNA). Scale bars, 20 µm. (C, D) Cells were stained with anti-histone H3pS10 antibody (for M phase) and PI for analyzing cell-cycle progression by flow cytometry. (C) Parental HeLa S3/TR, HeLa S3/TR/ATF7-wt (cl.2), or HeLa S3/TR/ATF7-TA (cl.1) cells were synchronized using DTB and released into thymidine-free medium containing 1 µg/ml Dox for 10.5~12.5 h. Two-dimensional histograms (DNA vs histone H3pS10) are presented together with DNA histograms, and the percentages of cells in G1 and M phases were measured. Cells in M and and G1 phases were quantitated from the results of S4 Fig. Values are means ± SD (three independent clones). Asterisks indicate the significant difference (*P<0.05; NS, not significant), as calculated by Student’s t-test. (D) Parental HeLa S3/TR, HeLa S3/TR/ATF7-wt (cl.2), or HeLa S3/TR/ATF7-TA (cl.1) cells were cultured in the presence of 9 µM RO-3306 for 10 h and treated with 1 µg/ml Dox for the last 5 h. The cells that were arrested at G2 phase were released into RO-3306-free medium containing 1 µg/ml Dox and incubated for 0, 10, and 20 min. Two-dimensional histograms (DNA vs histone H3pS10) are presented together with DNA histograms, and M-phase cells were quantitated. Values are means ± SD, n = 3 independent experiments. An asterisk indicates the significant difference (*P<0.05), as calculated by Student’s t-test.
From: Hasegawa H, Ishibashi K, Kubota S, Yamaguchi C, Yuki R, et al. (2014)
Cdk1-Mediated Phosphorylation of Human ATF7 at Thr-51 and Thr-53 Promotes Cell-Cycle Progression into M Phase.
PLoS ONE 9(12): e116048.
Rat anti tubulin-α antibody, clone YOL1/34 (MCA78G) used for the detection of tubulin-α in Drosophila by immunofluorescence.
Image caption:
Chromosomes remain associated into anaphase I of Cap-H2 mutants. Metaphase I and anaphase I morphologies were compared between wild-type and Cap-H2Z3-0019/Cap-H2TH1 mutant males. Testes were stained with DAPI and an anti-tubulin antibody to visualize DNA (white) and microtubules (green), respectively (scale bar in 3A indicates 10 μm and 5 μm in 3G). (A) Metaphase I in the wild-type. Each bivalent has congressed to the metaphase plate and appears as a cluster of DAPI stained material. (B) Anaphase I in the wild-type (DAPI only). Homologous chromosomes have segregated to daughter cells. (C) Anaphase I in the wild-type (DAPI and Tubulin merge). (D) Metaphase I from a Cap-H2Z3-0019/Cap-H2TH1 mutant male appears wild-type. (E) Anaphase I from a Cap-H2Z3-0019/Cap-H2TH1 mutant male (DAPI only). Chromatin bridges can be seen in three different segregation events. (F) Anaphase I from a Cap-H2Z3-0019/Cap-H2TH1 mutant male (DAPI and Tubulin merge).
From: Hartl TA, Sweeney SJ, Knepler PJ, Bosco G (2008)
Condensin II Resolves Chromosomal Associations to Enable Anaphase I Segregation in Drosophila Male Meiosis.
PLoS Genet 4(10): e1000228.
Image caption:
Cap-H2 mutants are defective in anaphase II segregation. Metaphase II and anaphase II morphologies were compared between wild-type and Cap-H2Z3-0019/Cap-H2TH1 mutant males. Testes were stained with DAPI and an anti-tubulin antibody to visualize DNA (white) and microtubules (green), respectively (scale bar in 6A indicates 10 μm). (A) Wild-type metaphase/anaphase II cyst. Metaphase II cells are those where each bivalent has congressed to the metaphase plate and appear as a cluster of DAPI staining material. Anaphase II are those cells with two DAPI staining white clusters, indicating homologous chromosome segregation. (B) Metaphase II and anaphase II figures from a Cap-H2 strong mutant. Arrow indicates an anaphase II bridge. The arrowhead highlights an anaphase II bridge or lagging chromosome.
From: Hartl TA, Sweeney SJ, Knepler PJ, Bosco G (2008)
Condensin II Resolves Chromosomal Associations to Enable Anaphase I Segregation in Drosophila Male Meiosis.
PLoS Genet 4(10): e1000228.
Image caption:
T566 phosphorylation affects Bub1 stability. (A) BUB1-T566A mutant cells do not show substantial delay in recovering from nocodazole arrest. Wild-type (WT) and BUB1-T566A mutant cells were incubated with nocodazole (15 μg/mL) at 30°C for 90 min and then released from nocodazole arrest; at the indicated times, samples were taken to measure rebudded cells. (B) BUB1-T566A mutant cells show no significant sensitivity to nocodazole in a survival assay. Wild-type (WT), bub1Δ, and BUB1-T566A cells were incubated with nocodazole (15 μg/mL); at the indicated times, cells were washed out and approximately 200 cells were plated on a YPD plate. Cell viability was calculated by dividing the number of colonies formed at the 2.5 and 5 h time points by that formed in the absence of nocodazole (0 h) at 30°C. (C) Phosphorylation of T566 is important for degradation of Bub1 during anaphase but not during G1. cdc15-2 cells with HA-tagged Bub1 or Bub1-T566A expressed by the GAL1 promoter (GAL-BUB1 and GAL-BUB1-T566A) were arrested in anaphase (cdc15-2) or in G1 (alpha-factor) and then transferred to medium containing galactose for 2 h to induce Bub1 expression. Glucose was added to shut-off Bub1 expression; samples were taken at the indicated times for Western blot analyses with antibody to the HA epitope. Tubulin was used as a loading control. (D) The Bub1-T566A protein is more stable than wild-type in the presence of nocodazole. Wild-type and BUB1-T566A mutant cells (Bub1 and Bub1-T566A are tagged with myc) were incubated in the presence of nocodazole (10 µg/mL) at 30°C; at the indicated times, samples were taken for Western blot analyses with antibody to the myc epitope. Tubulin was used as a loading control.
From: Goto GH, Mishra A, Abdulle R, Slaughter CA, Kitagawa K (2011)
Bub1-Mediated Adaptation of the Spindle Checkpoint.
PLoS Genet 7(1): e1001282.
Image caption:
Stages of Mitosis in Naegleria revealed by staining for α-tubulin, BN46/51 and DAPI. Images were obtained by conventional epifluorescence microscopy. A. Interphase; B. Prophase; C. Metaphase; D. Anaphase; E. Telophase. Bar = 10 μm. Red, BN46/51; Green, α-tubulin; Blue, DAPI.
Walsh CJ (2012)
The Structure of the Mitotic Spindle and Nucleolus during Mitosis in the Amebo-Flagellate Naegleria.
PLoS ONE 7(4): e34763.
Image caption:
Confocal Microscopy of Mitotic Cells Stained for α-Tubulin and the Nucleolar Protein BN46/51. Five examples of progressively later stages of each mitotic stage are presented. Each image is a Z-axis projection of 0.25 μm optical sections through an individual cell. The cell periphery is outlined in white. A. Interphase; B. Prophase; C. Metaphase; D. Anaphase; E. Telophase. F. Selected nuclei of, from left to right, Prophase, Metaphase, Anaphase, and Telophase. Bar = 10 μm. Red, BN 46/51; Green, α-tubulin.
From: Walsh CJ (2012)
The Structure of the Mitotic Spindle and Nucleolus during Mitosis in the Amebo-Flagellate Naegleria.
PLoS ONE 7(4): e34763.
Image caption:
Analysis of the Co-localization of Tubulin and the Nucleolar Protein BN46/51 During Prophase. Single 0.25 μm optical sections at 1.0 μm intervals are presented for two different cells. Columns A and D; raw data. Columns B and E; tubulin pixels are only displayed if the corresponding nucleolar protein pixel equaled or exceeded 25% of the maximum possible intensity. Columns C and F; tubulin pixels are only displayed if the corresponding nucleolar protein pixel equaled or exceeded 50% of maximum possible intensity. Numerical values are the summed fraction of tubulin intensity remaining in a given section after the subtraction. Red, BN 46/51; Green, α-tubulin. Bar = 10 μm.
From: Walsh CJ (2012)
The Structure of the Mitotic Spindle and Nucleolus during Mitosis in the Amebo-Flagellate Naegleria.
PLoS ONE 7(4): e34763.
Rat anti tubulin-α antibody, clone YOL1/34 (MCA78G) used as loading control for transfected yeast cell lysates by western blotting
Image caption:
Protein expression and solubility. Analysis of the expression and the soluble/insoluble partition of Aβwt-GFP and Aβm-GFP. The total, soluble and insoluble fractions were separated after induction. Tubulin alpha (Tubα) was employed to normalise the Aβ-GFP bands.
From: Sanchez de Groot N, Gomes RA, Villar-Pique A, Babu MM, Coelho AV,
Ventura S.
Proteome response at the edge of protein aggregation.
Open Biol. 2015 Feb;5(2). pii: 140221.
Rat anti Tubulin alpha antibody, clone YOL1/34 recognizes the alpha subunit of tubulin. The reactivity pattern is similar to that seen with clone YL1/2.
Rat anti Tubulin alpha antibody, clone YOL1/34 is routinely tested in ELISA on Tubulin.
Rat anti Tubulin alpha antibody, clone YOL1/34 is routinely tested in ELISA on Tubulin.
Product Details
- Target Species
- Yeast
- Species Cross-Reactivity
-
Target Species Cross Reactivity Birds Expected from Sequence Mammals Expected from Sequence Drosophila Fungal Expected from Sequence Human Arabidopsis Saccharomyces Platyzoma Ashbya Mouse Naegleria Asplenium nidus Seagrass (Cymodocea nodosa) - N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide - Carrier Free
- Yes
- Immunogen
- Yeast tubulin.
- Approx. Protein Concentrations
- IgG concentration 1.0mg/ml
- Fusion Partners
- Spleen cells from immunized LOU rats were fuzed with cells of the rat YB2/0 myeloma cell line.
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Shelf Life
- 18 months from date of despatch.
More Information
- Regulatory
- For research purposes only
Applications of Tubulin Alpha antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA | 10ug/ml as detecting antibody | ||
| Immunofluorescence | |||
| Immunohistology - Frozen | |||
| Radioimmunoassays | |||
| Western Blotting |
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
Copyright © 2018 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
| Description | Product Code | Pack Size | Applications | List Price | Quantity |
|---|---|---|---|---|---|
| Goat anti Rat IgG:Alk. Phos. (Mouse Adsorbed) | STAR131A | 1 ml | C E P WB | ||
| Goat anti Rat IgG:Biotin (Mouse Adsorbed) | STAR131B | 0.5 mg | C E IF P WB | ||
| Rabbit F(ab')2 anti Rat IgG:Dylight®800 | STAR16D800GA | 0.1 mg | F IF WB | ||
| Rabbit F(ab')2 anti Rat IgG:FITC | STAR17B | 1 mg | F | ||
| Rabbit F(ab')2 anti Rat IgG:HRP | STAR21B | 1 mg | C E P RE | ||
| Goat F(ab')2 anti Rat IgG:FITC (Mouse Adsorbed) | STAR69 | 0.5 ml | F | ||
| Goat anti Rat IgG:DyLight®649 (Mouse Adsorbed) | STAR71D649GA | 0.1 mg | F IF | ||
| Goat anti Rat IgG:Dylight®800 (Mouse Adsorbed) | STAR71D800GA | 0.1 mg | F IF WB | ||
| Goat anti Rat IgG:HRP (Mouse Adsorbed) | STAR72 | 0.5 mg | C E P | ||
| Goat F(ab')2 anti Rat IgG:RPE (Mouse Adsorbed) | STAR73 | 0.5 ml | F |
Product Specific References
References for Tubulin Alpha antibody
-
Kilmartin, J.V. et al. (1982) Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.
J Cell Biol. 93 (3): 576-82. -
Waples, W.G. et al. (2009) Putting the brake on FEAR: Tof2 promotes the biphasic release of Cdc14 phosphatase during mitotic exit.
Mol Biol Cell. 20 (1): 245-55. -
White, J. et al. (2005) Developmental activation of the Rb-E2F pathway and establishment of cell cycle-regulated cyclin-dependent kinase activity during embryonic stem cell differentiation.
Mol Biol Cell. 16 (4): 2018-27. -
Lang, C. et al. (2010) Structural mutants of the spindle pole body cause distinct alteration of cytoplasmic microtubules and nuclear dynamics in multinucleated hyphae.
Mol Biol Cell. 21 (5): 753-66. -
Hao, N. et al. (2011) Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR.
Nucleic Acids Res. 39 (9): 3695-709. -
D'Ambrosio, C. et al. (2008) Identification of cis-acting sites for condensin loading onto budding yeast chromosomes.
Genes Dev. 22: 2215-27 -
Hartl, T.A. et al. (2008) Condensin II resolves chromosomal associations to enable anaphase I segregation in Drosophila male meiosis.
PLoS Genet. 4: e1000228. -
Mirchenko, L. and Uhlmann, F. (2010) Sli15(INCENP) dephosphorylation prevents mitotic checkpoint reengagement due to loss of tension at anaphase onset.
Curr Biol. 20: 1396-401. -
Sullivan, M. et al. (2001) Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19.
Nat Cell Biol. 3: 771-7. -
Sullivan, M. et al. (2008) Cyclin-specific control of ribosomal DNA segregation.
Mol Cell Biol. 28: 5328-36. -
Yu, H.G. et al. (2007) The Aurora kinase Ipl1 maintains the centromeric localization of PP2A to protect cohesin during meiosis.
J Cell Biol. 176: 911-8. -
Rossio, V. and Yoshida, S. (2011) Spatial regulation of Cdc55-PP2A by Zds1/Zds2 controls mitotic entry and mitotic exit in budding yeast.
J Cell Biol. 193: 445-54. -
Grava, S. et al. (2011) Clustering of Nuclei in Multinucleated Hyphae Is Prevented by Dynein-Driven Bidirectional Nuclear Movements and Microtubule Growth Control in Ashbya gossypii.
Eukaryot Cell. 10: 902-15. -
Raspelli, E. et al. (2011) Budding yeast Dma1 and Dma2 participate in regulation of Swe1 levels and localization.
Mol Biol Cell. 22: 2185-97. -
Finlayson, M.R. et al. (2011) Regulation of exit from mitosis in multinucleate Ashbya gossypii cells relies on a minimal network of genes.
Mol Biol Cell. 22 (17): 3081-93. -
Chatzimeletiou, K. et al. (2005) Spindle abnormalities in normally developing and arrested human preimplantation embryos in vitro identified by confocal laser scanning microscopy.
Hum Reprod. 20: 672-82. -
Chatzimeletiou, K. et al. (2012) Cytoskeletal analysis of human blastocysts by confocal laser scanning microscopy following vitrification.
Hum Reprod. 27: 106-13. -
Keeling, J.W. and Miller, R.K. (2011) Indirect immunofluorescence for monitoring spindle assembly and disassembly in yeast.
Methods Mol Biol. 782: 231-44. -
Elhanany-Tamir, H. et al. (2012) Organelle positioning in muscles requires cooperation between two KASH proteins and microtubules.
J Cell Biol. 198 (5): 833-46. -
Walsh, C.J. (2012) The structure of the mitotic spindle and nucleolus during mitosis in the amebo-flagellate Naegleria.
PLoS One. 7: e34763. -
Adamakis, I.D. et al. (2013) Effects of bisphenol A on the microtubule arrays in root meristematic cells of Pisum sativum L.
Mutat Res. 750 (1-2): 111-20. -
Buerstenbinder, K. et al. (2013) Arabidopsis Calmodulin-binding IQD1 Localizes to Microtubules and Interacts with Kinesin Light Chain-Related Protein-1.
J Biol Chem. 288: 1871-82. -
Panteris, E. et al. (2013) The distribution of TPX2 in dividing leaf cells of the fern Asplenium nidus.
Plant Biol (Stuttg). 15: 203-9. -
Malea, P. et al. (2013) Microtubule integrity and cell viability under metal (Cu, Ni and Cr) stress in the seagrass Cymodocea nodosa.
Chemosphere. pii: S0045-6535(13)00820-5. -
Eleftheriou, E.P. et al. (2016) Hexavalent chromium-induced differential disruption of cortical microtubules in some Fabaceae species is correlated with acetylation of α-tubulin.
Protoplasma. 253 (2): 531-42. -
Wang, S. et al. (2015) Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1.
J Cell Biol. 209 (4): 529-38. -
Okamoto, M. et al. (2016) Fyn Accelerates M Phase Progression by Promoting the Assembly of Mitotic Spindle Microtubules.
J Cell Biochem. 117 (4): 894-903. -
Eleftheriou, E.P. et al. (2015) Aberration of mitosis by hexavalent chromium in some Fabaceae members is mediated by species-specific microtubule disruption.
Environ Sci Pollut Res Int. 22 (10): 7590-9. -
Sullivan, A.E. et al. (2016) MAGED1 is a novel regulator of a select subset of bHLH PAS transcription factors.
FEBS J. 283 (18): 3488-502. -
Schweizer, N. et al. (2015) An organelle-exclusion envelope assists mitosis and underlies distinct molecular crowding in the spindle region.
J Cell Biol. 210 (5): 695-704. -
Livanos P et al. (2016) Deliberate ROS production and auxin synergistically trigger the asymmetrical division generating the subsidiary cells in Zea mays stomatal complexes.
Protoplasma. 253 (4): 1081-99. -
Xie, J.L. et al. (2017) Staurosporine Induces Filamentation in the Human Fungal Pathogen Candida albicans via Signaling through Cyr1 and Protein Kinase A.
mSphere. 2 (2): Mar 1;2(2). pii: e00056-17. eCollection 2017 Mar-Apr. -
Bacon, T. et al. (2015) Histone deacetylase 3 indirectly modulates tubulin acetylation.
Biochem J. 472 (3): 367-77. -
Kowanda, M. et al. (2016) Loss of function of the Drosophila Ninein-related centrosomal protein Bsg25D causes mitotic defects and impairs embryonic development.
Biol Open. 5 (8): 1040-51. -
Diao, L.T. et al. (2017) Delineation of the role of chromatin assembly and the Rtt101Mms1 E3 ubiquitin ligase in DNA damage checkpoint recovery in budding yeast.
PLoS One. 12 (7): e0180556.
