HeLa cells stained with Rat anti tubulin apha (MCA78G) green, nuclei are counterstained with DAPI

Western blot analysis of CD107b on J774 cell lysate probed with Rat anti Mouse CD107b (MCA2293) at 1/500, 1/1000, 1/2000. Rat anti tubulin alpha (MCA78G) is included as a loading control. Detection is with Goat anti Rat IgG:Dylight^®(STAR71D800GA)

Published customer image:
Rat anti tubulin-α antibody 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-a-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.

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Rat anti tubulin-α antibody 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). (G) Higher resolution wild-type anaphase I image showing complete segregation of homologs. (H) Anaphase I from a Cap-H2Z3-0019/Cap-H2TH1 mutant demonstrating extensive chromatin bridging due to persistent associations between chromosomes migrating to opposing poles. (I) Anaphase I bridge found from a Cap-D3EY00456 mutant.

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.

Published customer image:Rat anti tubulin-α antibody used for the detection of tubulin-α in Drosophila by immunofluorescence.
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.

Published customer image:Rat anti tubulin-α antibody used for the detection of tubulin-α as a loading control for yeast cell lysates by western blotting
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), bub1?, 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.

Published customer image:Rat anti tubulin-α antibody used for the detection of tubulin-α in the amebo-flagellate Naegleria sp. by immunofluorescence.
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.

Published customer image:Rat anti tubulin-α antibody used for the detection of tubulin-α in the amebo-flagellate Naegleria sp. by immunofluorescence.
Image caption:
Confocal Microscopy of Mitotic Cells Stained for a-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, a-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.

Published customer image:Rat anti tubulin-α antibody used for the detection of tubulin-α in the amebo-flagellate Naegleria sp. by immunofluorescence.
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, a-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.

Published customer image:
Rat anti tubulin-α antibody 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.