rat anti tubulin  (Novus Biologicals)

 
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    Name:
    beta III Tubulin Overexpression Lysate Denatured
    Description:

    Catalog Number:
    H00010381-T02
    Price:
    299
    Category:
    Lysates
    Size:
    0 1 ml
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    Structured Review

    Novus Biologicals rat anti tubulin
    beta III Tubulin Overexpression Lysate Denatured

    https://www.bioz.com/result/rat anti tubulin/product/Novus Biologicals
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rat anti tubulin - by Bioz Stars, 2021-09
    91/100 stars

    Images

    1) Product Images from "Ipl1/Aurora Kinase Suppresses S-CDK-Driven Spindle Formation during Prophase I to Ensure Chromosome Integrity during Meiosis"

    Article Title: Ipl1/Aurora Kinase Suppresses S-CDK-Driven Spindle Formation during Prophase I to Ensure Chromosome Integrity during Meiosis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0083982

    Ipl1 prevents formation of spindles in DDR-arrested cells. (A) Proportion of cells with separated spindle-pole bodies as a function of time. Strains: Wild type (Y940), ipl1-md (Y1206), dmc1 Δ (Y2266), ipl1-md dmc1 Δ (Y2268), hop2 Δ (Y2489), hop2 Δ ip1-mn (Y2491) rec8 Δ (Y2404), rec8 Δ ipl1-md (Y2457). Three independent diploids were assessed, a representative time course is shown for each strain. (B, C) Tubulin configurations observed in dmc1 Δ ipl1-md mutants and their prevalence (C). (D) Representative examples of spindle configurations from a single frame (maximum intensity projection) from time lapse imaging in dmc1 Δ and dmc1 Δ ipl1-md mutants. (E) The cumulative proportion of cells that formed spindles during the three hours of time-lapse imaging (8–11 h). (F) Representative example dynamic behaviour of tubulin (Tub1-GFP) and DNA (H2B-mCherry) during time-lapse imaging of the dmc1 Δ ipl1-md mutant. (G) Western blot showing that Ipl1 is efficiently depleted in dmc1 Δ ipl1-md cells.
    Figure Legend Snippet: Ipl1 prevents formation of spindles in DDR-arrested cells. (A) Proportion of cells with separated spindle-pole bodies as a function of time. Strains: Wild type (Y940), ipl1-md (Y1206), dmc1 Δ (Y2266), ipl1-md dmc1 Δ (Y2268), hop2 Δ (Y2489), hop2 Δ ip1-mn (Y2491) rec8 Δ (Y2404), rec8 Δ ipl1-md (Y2457). Three independent diploids were assessed, a representative time course is shown for each strain. (B, C) Tubulin configurations observed in dmc1 Δ ipl1-md mutants and their prevalence (C). (D) Representative examples of spindle configurations from a single frame (maximum intensity projection) from time lapse imaging in dmc1 Δ and dmc1 Δ ipl1-md mutants. (E) The cumulative proportion of cells that formed spindles during the three hours of time-lapse imaging (8–11 h). (F) Representative example dynamic behaviour of tubulin (Tub1-GFP) and DNA (H2B-mCherry) during time-lapse imaging of the dmc1 Δ ipl1-md mutant. (G) Western blot showing that Ipl1 is efficiently depleted in dmc1 Δ ipl1-md cells.

    Techniques Used: Imaging, Mutagenesis, Western Blot

    S-CDK is required and sufficient to drive SPB separation and spindle formation during prophase I in ipl1-md cells. (A)Images for tubulin and Zip1 staining in dmc1 Δ ipl1-md strains with normal S-CDK and M-CDK (left image), lacking S-CDK activity ( clb5 Δ clb6 Δ; middle image), or without M-CDK proficient for Clb5 only ( clb1 Δ, clb3 Δ, clb4 Δ, clb6 Δ CLB5 + ; right panel). Strains: Y4495, Y4435, and Y4496, respectively. Bars, 2 µm. (B) Quantification on the proportion of fixed cells with spindles and separated SPBs at 8 hours and 12 hours. (C, D) ipl1-md ndt80 Δ cdc28-as1 (Y2577) cells were treated with either 50 µM 1-NM-PP1 (+) or solvent only (DMSO) (−) to inhibit Cdc28/CDK kinase activity at 6 hours, when spindles have formed in at least 20% of ipl1-md ndt80 Δ cells. Examples of spread, meiotic nuclei are shown to the left. Note that there was no effect on inhibiting Cdc28-as1 in ndt80 Δ alone bars, 2 µm. The graph shows that Quantification of prophase spreads with spindles or aberrant spindle pole structures ( e.g. multipolar spindles).
    Figure Legend Snippet: S-CDK is required and sufficient to drive SPB separation and spindle formation during prophase I in ipl1-md cells. (A)Images for tubulin and Zip1 staining in dmc1 Δ ipl1-md strains with normal S-CDK and M-CDK (left image), lacking S-CDK activity ( clb5 Δ clb6 Δ; middle image), or without M-CDK proficient for Clb5 only ( clb1 Δ, clb3 Δ, clb4 Δ, clb6 Δ CLB5 + ; right panel). Strains: Y4495, Y4435, and Y4496, respectively. Bars, 2 µm. (B) Quantification on the proportion of fixed cells with spindles and separated SPBs at 8 hours and 12 hours. (C, D) ipl1-md ndt80 Δ cdc28-as1 (Y2577) cells were treated with either 50 µM 1-NM-PP1 (+) or solvent only (DMSO) (−) to inhibit Cdc28/CDK kinase activity at 6 hours, when spindles have formed in at least 20% of ipl1-md ndt80 Δ cells. Examples of spread, meiotic nuclei are shown to the left. Note that there was no effect on inhibiting Cdc28-as1 in ndt80 Δ alone bars, 2 µm. The graph shows that Quantification of prophase spreads with spindles or aberrant spindle pole structures ( e.g. multipolar spindles).

    Techniques Used: Staining, Activity Assay

    Ipl1 depletion causes precocious formation of spindles in prophase I-arrested ndt80 mutants. (A) Representative examples of SPB and spindle configurations in ndt80 Δ and ndt80 Δ ipl1-md mutants. (B) The proportion of cells that formed spindles during the four hours of time-lapse imaging. A small number multipolar spindles were observed; these were added to the ‘spindle’ category. (C) Representative example dynamic behaviour of tubulin during time-lapse imaging of the ndt80 Δ ipl1-md mutant. (D) Spindle formation in ipl1-md cells arrested in prophase I (t = 0; 6 hours in sporulation medium), and after release using the ndt80-IN system (WT: Y967 and ipl1-mn :Y1169). The spindle and SPB conformation were assessed in > 100 cells every 15 min. after release from NDT80 arrest.
    Figure Legend Snippet: Ipl1 depletion causes precocious formation of spindles in prophase I-arrested ndt80 mutants. (A) Representative examples of SPB and spindle configurations in ndt80 Δ and ndt80 Δ ipl1-md mutants. (B) The proportion of cells that formed spindles during the four hours of time-lapse imaging. A small number multipolar spindles were observed; these were added to the ‘spindle’ category. (C) Representative example dynamic behaviour of tubulin during time-lapse imaging of the ndt80 Δ ipl1-md mutant. (D) Spindle formation in ipl1-md cells arrested in prophase I (t = 0; 6 hours in sporulation medium), and after release using the ndt80-IN system (WT: Y967 and ipl1-mn :Y1169). The spindle and SPB conformation were assessed in > 100 cells every 15 min. after release from NDT80 arrest.

    Techniques Used: Imaging, Mutagenesis

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    Article Snippet: Antibodies used were mouse anti-αvβ3 integrin (LM609), rabbit anti-β3 integrin, mouse anti-αv integrin (Chemicon, Temecula, CA), mouse anti-β5 integrin (Calbiochem, San Diego, CA), goat anti-β3 integrin (N-20) (Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-FAK [pY397] (Invitrogen, Carlsbad, CA), rabbit monoclonal anti-paxillin (Epitomics, Burlingame, CA), rabbit monoclonal anti-plectin (Epitomics), rabbit anti-dynein heavy chain (Santa Cruz Biotechnology), mouse anti-kinesin heavy chain (Chemicon), rabbit monoclonal anti-actin (Epitomics), rat monoclonal anti-tubulin (Novus Biologicals, Littleton, CO), rabbit anti-mTOR (Cell Signaling Technology, Danvers, MA), mouse anti-vimentin (V9) (Sigma), and rhodamine-conjugated phalloidin (Molecular Probes, Eugene, OR).

    Immunostaining:

    Article Title: α-Synuclein in gut endocrine cells and its implications for Parkinson’s disease
    Article Snippet: .. When cells had reached the desired confluency, they were washed with PBS and fixed for 10 minutes in 10% formalin. β-Tubulin polyclonal antibody raised in rabbit (Novus Biologicals LLC) and mouse α-synuclein antibody (BD Transduction Laboratories) were used for immunostaining as described below. ..

    Derivative Assay:

    Article Title: Loss of hepatic aryl hydrocarbon receptor protein in adrenalectomized rats does not involve altered levels of the receptor's cytoplasmic chaperones
    Article Snippet: .. Blots derived from gels originally loaded with 20 or 25 μg of hepatic cytosolic protein were probed with the following primary antibodies: mouse monoclonal against human AIP, dilution 1:10,000 (Dr. Christopher A. Bradfield, McArdle Laboratory for Cancer Research, Madison, WI); mouse monoclonal against a human hsp90β peptide, dilution 1:50,000 (Santa Cruz Biotechnology, Santa Cruz, CA); mouse monoclonal against a human p23 peptide, dilution 1:2,000 (Santa Cruz Biotechnology); and mouse monoclonal against pig β-tubulin, dilution 1:10,000 (Novus Biologicals, Littleton, CO). ..

    Imaging:

    Article Title: Metabolic Maintenance of Cell Asymmetry following Division in Activated T Lymphocytes
    Article Snippet: .. T Cell Imaging Antibodies against the following antigens were used: CD8 (13-0081-85; eBioscience), β-tubulin (T8328; Sigma-Aldrich), Numb (ab14140; Abcam), Scribble (ab154067; Abcam), PKCζ (IMG-90589-2; Imgenex), c-Myc (9402; Cell Signaling), pS6 (5364; Cell Signaling), p70S6K (9234; Cell Signaling), pmTOR (2974; Cell Signaling), pS256 FOXO1 (9461; Cell Signaling), CD98-PE (12-0981-81; eBiosciences), SLC1A5 (ARP42247_T100; AVIVA), and SLC1A3 (ABIN377559; antibodiesonline). ..

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  • 93
    Novus Biologicals β tubulin
    Activation of UPR and ER stress in the naturally and prematurely aged gastrocnemius muscle. (a) Western blot analyses of the three UPR pathway markers, namely PERK‐eIF2α, IRE1‐XBP1, and ATF6. <t>β‐Tubulin</t> in the ATF6 blot is shown as the representative internal control. See Fig. S5 b–d for three complete blots. (b) Quantification of the p‐eIF2α and total eIF2α and the ratio of p‐eIF2α/total eIF2α. * p
    β Tubulin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β tubulin/product/Novus Biologicals
    Average 93 stars, based on 1 article reviews
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    91
    Novus Biologicals rat anti tubulin
    Ipl1 prevents formation of spindles in DDR-arrested cells. (A) Proportion of cells with separated spindle-pole bodies as a function of time. Strains: Wild type (Y940), ipl1-md (Y1206), dmc1 Δ (Y2266), ipl1-md dmc1 Δ (Y2268), hop2 Δ (Y2489), hop2 Δ ip1-mn (Y2491) rec8 Δ (Y2404), rec8 Δ ipl1-md (Y2457). Three independent diploids were assessed, a representative time course is shown for each strain. (B, C) <t>Tubulin</t> configurations observed in dmc1 Δ ipl1-md mutants and their prevalence (C). (D) Representative examples of spindle configurations from a single frame (maximum intensity projection) from time lapse imaging in dmc1 Δ and dmc1 Δ ipl1-md mutants. (E) The cumulative proportion of cells that formed spindles during the three hours of time-lapse imaging (8–11 h). (F) Representative example dynamic behaviour of tubulin (Tub1-GFP) and DNA (H2B-mCherry) during time-lapse imaging of the dmc1 Δ ipl1-md mutant. (G) Western blot showing that Ipl1 is efficiently depleted in dmc1 Δ ipl1-md cells.
    Rat Anti Tubulin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Novus Biologicals anti tubulin
    Zoom scan ion abundance mass spectra for ICAT labeled tryptic peptides from actin and A32A (cytosol) and <t>tubulin</t> and COXG (membranes). The spectra demonstrate the similarities in ion abundances found for the tryptic peptides using cICAT labeling as compared
    Anti Tubulin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Novus Biologicals mouse monoclonal anti tubulin
    Specificity of pAb506P. (A) Comparative titration curves of pAb506P on ELISA plates coated with a topo I peptide surrounding the serine 506 site, either in its phosphorylated or non-phosphorylated form. (B) Western analyses of H358 cell lysates (100 μg/lane) probed with pAb506P (lane 1) or with goat anti-topo I (lane 2). Arrows indicate positions of the 45 kDa species and full length topo I. (C) Topo I immunoprecipitation (goat anti-topo I C-terminus) followed by pAb506P Western of H358 cell lysates. Lane represents 200 μg starting material. (D) Western analysis of PS506 and actin in H358 cell lysates before (cntr) and after treatment with alkaline phosphatase (AP). (E) Western analysis of PS506 (using pAb506P), full length topo I (using goat anti-topo I) and <t>tubulin</t> in H358 cells before and after a 24 hr treatment of cells with 0.1 or 1 μM CPT.
    Mouse Monoclonal Anti Tubulin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Activation of UPR and ER stress in the naturally and prematurely aged gastrocnemius muscle. (a) Western blot analyses of the three UPR pathway markers, namely PERK‐eIF2α, IRE1‐XBP1, and ATF6. β‐Tubulin in the ATF6 blot is shown as the representative internal control. See Fig. S5 b–d for three complete blots. (b) Quantification of the p‐eIF2α and total eIF2α and the ratio of p‐eIF2α/total eIF2α. * p

    Journal: Aging Cell

    Article Title: Comparative proteomic profiling reveals a role for Cisd2 in skeletal muscle aging, et al. Comparative proteomic profiling reveals a role for Cisd2 in skeletal muscle aging

    doi: 10.1111/acel.12705

    Figure Lengend Snippet: Activation of UPR and ER stress in the naturally and prematurely aged gastrocnemius muscle. (a) Western blot analyses of the three UPR pathway markers, namely PERK‐eIF2α, IRE1‐XBP1, and ATF6. β‐Tubulin in the ATF6 blot is shown as the representative internal control. See Fig. S5 b–d for three complete blots. (b) Quantification of the p‐eIF2α and total eIF2α and the ratio of p‐eIF2α/total eIF2α. * p

    Article Snippet: 4.7 Western blotting The following antibodies were used for Western blotting: Cisd2 (Chen et al., ); β‐tubulin (05‐661; Upstate); ATF‐6α (IMG‐273; Imgenex); eIF2α (#9722; Cell Signaling); p‐eIF2α (Ser51, #3398; Cell Signaling); IRE1α (#3294; Cell Signaling); p‐IRE1α (Ser724, PA1‐16927; Thermo); 3‐Nitrotyrosine (ab61392; Abcam); Cysteine (sulfonate) (ADI‐OSA‐820; Enzo); and Serca1 (MA3‐912; Thermo).

    Techniques: Activation Assay, Western Blot

    Decreased activity of Serca1 and increased oxidative stress in naturally and prematurely aged gastrocnemius muscle. (a) Significant reductions occurred in calcium‐dependent Serca ATPase activity in naturally aged (26M) WT and prematurely aged (3M) Cisd2 mKO mice. The selective Serca pump inhibitor, TBQ, was used to reflect a specific difference in Serca activity. n = 4 for each group of mice. (b) Increased cysteine S‐sulfonation and tyrosine nitration on Serca1 protein in gastrocnemius muscles. The total Serca1 protein was detected by re‐blotting on the same membrane. (c,d) Increase in oxidative modifications, namely S‐sulfonated cysteine and 3‐nitrotyrosine, for all proteins present in whole cell extracts of the gastrocnemius muscle. Quantification of each sample was based on the entire intensities of each lane or region normalized to β‐tubulin. *p

    Journal: Aging Cell

    Article Title: Comparative proteomic profiling reveals a role for Cisd2 in skeletal muscle aging, et al. Comparative proteomic profiling reveals a role for Cisd2 in skeletal muscle aging

    doi: 10.1111/acel.12705

    Figure Lengend Snippet: Decreased activity of Serca1 and increased oxidative stress in naturally and prematurely aged gastrocnemius muscle. (a) Significant reductions occurred in calcium‐dependent Serca ATPase activity in naturally aged (26M) WT and prematurely aged (3M) Cisd2 mKO mice. The selective Serca pump inhibitor, TBQ, was used to reflect a specific difference in Serca activity. n = 4 for each group of mice. (b) Increased cysteine S‐sulfonation and tyrosine nitration on Serca1 protein in gastrocnemius muscles. The total Serca1 protein was detected by re‐blotting on the same membrane. (c,d) Increase in oxidative modifications, namely S‐sulfonated cysteine and 3‐nitrotyrosine, for all proteins present in whole cell extracts of the gastrocnemius muscle. Quantification of each sample was based on the entire intensities of each lane or region normalized to β‐tubulin. *p

    Article Snippet: 4.7 Western blotting The following antibodies were used for Western blotting: Cisd2 (Chen et al., ); β‐tubulin (05‐661; Upstate); ATF‐6α (IMG‐273; Imgenex); eIF2α (#9722; Cell Signaling); p‐eIF2α (Ser51, #3398; Cell Signaling); IRE1α (#3294; Cell Signaling); p‐IRE1α (Ser724, PA1‐16927; Thermo); 3‐Nitrotyrosine (ab61392; Abcam); Cysteine (sulfonate) (ADI‐OSA‐820; Enzo); and Serca1 (MA3‐912; Thermo).

    Techniques: Activity Assay, Mouse Assay, Nitration

    Ipl1 prevents formation of spindles in DDR-arrested cells. (A) Proportion of cells with separated spindle-pole bodies as a function of time. Strains: Wild type (Y940), ipl1-md (Y1206), dmc1 Δ (Y2266), ipl1-md dmc1 Δ (Y2268), hop2 Δ (Y2489), hop2 Δ ip1-mn (Y2491) rec8 Δ (Y2404), rec8 Δ ipl1-md (Y2457). Three independent diploids were assessed, a representative time course is shown for each strain. (B, C) Tubulin configurations observed in dmc1 Δ ipl1-md mutants and their prevalence (C). (D) Representative examples of spindle configurations from a single frame (maximum intensity projection) from time lapse imaging in dmc1 Δ and dmc1 Δ ipl1-md mutants. (E) The cumulative proportion of cells that formed spindles during the three hours of time-lapse imaging (8–11 h). (F) Representative example dynamic behaviour of tubulin (Tub1-GFP) and DNA (H2B-mCherry) during time-lapse imaging of the dmc1 Δ ipl1-md mutant. (G) Western blot showing that Ipl1 is efficiently depleted in dmc1 Δ ipl1-md cells.

    Journal: PLoS ONE

    Article Title: Ipl1/Aurora Kinase Suppresses S-CDK-Driven Spindle Formation during Prophase I to Ensure Chromosome Integrity during Meiosis

    doi: 10.1371/journal.pone.0083982

    Figure Lengend Snippet: Ipl1 prevents formation of spindles in DDR-arrested cells. (A) Proportion of cells with separated spindle-pole bodies as a function of time. Strains: Wild type (Y940), ipl1-md (Y1206), dmc1 Δ (Y2266), ipl1-md dmc1 Δ (Y2268), hop2 Δ (Y2489), hop2 Δ ip1-mn (Y2491) rec8 Δ (Y2404), rec8 Δ ipl1-md (Y2457). Three independent diploids were assessed, a representative time course is shown for each strain. (B, C) Tubulin configurations observed in dmc1 Δ ipl1-md mutants and their prevalence (C). (D) Representative examples of spindle configurations from a single frame (maximum intensity projection) from time lapse imaging in dmc1 Δ and dmc1 Δ ipl1-md mutants. (E) The cumulative proportion of cells that formed spindles during the three hours of time-lapse imaging (8–11 h). (F) Representative example dynamic behaviour of tubulin (Tub1-GFP) and DNA (H2B-mCherry) during time-lapse imaging of the dmc1 Δ ipl1-md mutant. (G) Western blot showing that Ipl1 is efficiently depleted in dmc1 Δ ipl1-md cells.

    Article Snippet: Rat anti-tubulin (YOL034W (1∶400, Novus Biologicals).

    Techniques: Imaging, Mutagenesis, Western Blot

    S-CDK is required and sufficient to drive SPB separation and spindle formation during prophase I in ipl1-md cells. (A)Images for tubulin and Zip1 staining in dmc1 Δ ipl1-md strains with normal S-CDK and M-CDK (left image), lacking S-CDK activity ( clb5 Δ clb6 Δ; middle image), or without M-CDK proficient for Clb5 only ( clb1 Δ, clb3 Δ, clb4 Δ, clb6 Δ CLB5 + ; right panel). Strains: Y4495, Y4435, and Y4496, respectively. Bars, 2 µm. (B) Quantification on the proportion of fixed cells with spindles and separated SPBs at 8 hours and 12 hours. (C, D) ipl1-md ndt80 Δ cdc28-as1 (Y2577) cells were treated with either 50 µM 1-NM-PP1 (+) or solvent only (DMSO) (−) to inhibit Cdc28/CDK kinase activity at 6 hours, when spindles have formed in at least 20% of ipl1-md ndt80 Δ cells. Examples of spread, meiotic nuclei are shown to the left. Note that there was no effect on inhibiting Cdc28-as1 in ndt80 Δ alone bars, 2 µm. The graph shows that Quantification of prophase spreads with spindles or aberrant spindle pole structures ( e.g. multipolar spindles).

    Journal: PLoS ONE

    Article Title: Ipl1/Aurora Kinase Suppresses S-CDK-Driven Spindle Formation during Prophase I to Ensure Chromosome Integrity during Meiosis

    doi: 10.1371/journal.pone.0083982

    Figure Lengend Snippet: S-CDK is required and sufficient to drive SPB separation and spindle formation during prophase I in ipl1-md cells. (A)Images for tubulin and Zip1 staining in dmc1 Δ ipl1-md strains with normal S-CDK and M-CDK (left image), lacking S-CDK activity ( clb5 Δ clb6 Δ; middle image), or without M-CDK proficient for Clb5 only ( clb1 Δ, clb3 Δ, clb4 Δ, clb6 Δ CLB5 + ; right panel). Strains: Y4495, Y4435, and Y4496, respectively. Bars, 2 µm. (B) Quantification on the proportion of fixed cells with spindles and separated SPBs at 8 hours and 12 hours. (C, D) ipl1-md ndt80 Δ cdc28-as1 (Y2577) cells were treated with either 50 µM 1-NM-PP1 (+) or solvent only (DMSO) (−) to inhibit Cdc28/CDK kinase activity at 6 hours, when spindles have formed in at least 20% of ipl1-md ndt80 Δ cells. Examples of spread, meiotic nuclei are shown to the left. Note that there was no effect on inhibiting Cdc28-as1 in ndt80 Δ alone bars, 2 µm. The graph shows that Quantification of prophase spreads with spindles or aberrant spindle pole structures ( e.g. multipolar spindles).

    Article Snippet: Rat anti-tubulin (YOL034W (1∶400, Novus Biologicals).

    Techniques: Staining, Activity Assay

    Ipl1 depletion causes precocious formation of spindles in prophase I-arrested ndt80 mutants. (A) Representative examples of SPB and spindle configurations in ndt80 Δ and ndt80 Δ ipl1-md mutants. (B) The proportion of cells that formed spindles during the four hours of time-lapse imaging. A small number multipolar spindles were observed; these were added to the ‘spindle’ category. (C) Representative example dynamic behaviour of tubulin during time-lapse imaging of the ndt80 Δ ipl1-md mutant. (D) Spindle formation in ipl1-md cells arrested in prophase I (t = 0; 6 hours in sporulation medium), and after release using the ndt80-IN system (WT: Y967 and ipl1-mn :Y1169). The spindle and SPB conformation were assessed in > 100 cells every 15 min. after release from NDT80 arrest.

    Journal: PLoS ONE

    Article Title: Ipl1/Aurora Kinase Suppresses S-CDK-Driven Spindle Formation during Prophase I to Ensure Chromosome Integrity during Meiosis

    doi: 10.1371/journal.pone.0083982

    Figure Lengend Snippet: Ipl1 depletion causes precocious formation of spindles in prophase I-arrested ndt80 mutants. (A) Representative examples of SPB and spindle configurations in ndt80 Δ and ndt80 Δ ipl1-md mutants. (B) The proportion of cells that formed spindles during the four hours of time-lapse imaging. A small number multipolar spindles were observed; these were added to the ‘spindle’ category. (C) Representative example dynamic behaviour of tubulin during time-lapse imaging of the ndt80 Δ ipl1-md mutant. (D) Spindle formation in ipl1-md cells arrested in prophase I (t = 0; 6 hours in sporulation medium), and after release using the ndt80-IN system (WT: Y967 and ipl1-mn :Y1169). The spindle and SPB conformation were assessed in > 100 cells every 15 min. after release from NDT80 arrest.

    Article Snippet: Rat anti-tubulin (YOL034W (1∶400, Novus Biologicals).

    Techniques: Imaging, Mutagenesis

    Zoom scan ion abundance mass spectra for ICAT labeled tryptic peptides from actin and A32A (cytosol) and tubulin and COXG (membranes). The spectra demonstrate the similarities in ion abundances found for the tryptic peptides using cICAT labeling as compared

    Journal: Journal of proteome research

    Article Title: Quantitative Protein Expression Analysis Of CLL B Cells from Mutated and Unmutated IgVH Subgroups Using Acid-Cleavable Isotope-Coded Affinity Tag Reagents

    doi: 10.1021/pr050028f

    Figure Lengend Snippet: Zoom scan ion abundance mass spectra for ICAT labeled tryptic peptides from actin and A32A (cytosol) and tubulin and COXG (membranes). The spectra demonstrate the similarities in ion abundances found for the tryptic peptides using cICAT labeling as compared

    Article Snippet: The primary antibodies used include the following; anti-actin, mouse mAb 1:5000 dilution (Novus Biologicals, Littleton, CO, Cat# NB 600-501), anti-A32A, rabbit polyclonal Ab 1:2,500 dilution (Novus Biologicals, Littleton, CO, Cat# ab5989), anti-tubulin, mouse mAb 1:5,000 dilution (Novus Biologicals, Littleton, CO, Cat# ab7291), anti-COXVIb, mouse mAb 1:5,000 dilution (Molecular Probes, Inc., Eugene, OR, Cat# ).

    Techniques: Labeling

    Specificity of pAb506P. (A) Comparative titration curves of pAb506P on ELISA plates coated with a topo I peptide surrounding the serine 506 site, either in its phosphorylated or non-phosphorylated form. (B) Western analyses of H358 cell lysates (100 μg/lane) probed with pAb506P (lane 1) or with goat anti-topo I (lane 2). Arrows indicate positions of the 45 kDa species and full length topo I. (C) Topo I immunoprecipitation (goat anti-topo I C-terminus) followed by pAb506P Western of H358 cell lysates. Lane represents 200 μg starting material. (D) Western analysis of PS506 and actin in H358 cell lysates before (cntr) and after treatment with alkaline phosphatase (AP). (E) Western analysis of PS506 (using pAb506P), full length topo I (using goat anti-topo I) and tubulin in H358 cells before and after a 24 hr treatment of cells with 0.1 or 1 μM CPT.

    Journal: PLoS ONE

    Article Title: Topoisomerase-I PS506 as a Dual Function Cancer Biomarker

    doi: 10.1371/journal.pone.0134929

    Figure Lengend Snippet: Specificity of pAb506P. (A) Comparative titration curves of pAb506P on ELISA plates coated with a topo I peptide surrounding the serine 506 site, either in its phosphorylated or non-phosphorylated form. (B) Western analyses of H358 cell lysates (100 μg/lane) probed with pAb506P (lane 1) or with goat anti-topo I (lane 2). Arrows indicate positions of the 45 kDa species and full length topo I. (C) Topo I immunoprecipitation (goat anti-topo I C-terminus) followed by pAb506P Western of H358 cell lysates. Lane represents 200 μg starting material. (D) Western analysis of PS506 and actin in H358 cell lysates before (cntr) and after treatment with alkaline phosphatase (AP). (E) Western analysis of PS506 (using pAb506P), full length topo I (using goat anti-topo I) and tubulin in H358 cells before and after a 24 hr treatment of cells with 0.1 or 1 μM CPT.

    Article Snippet: Mouse monoclonal anti-tubulin was purchased from Novus Biologicals (Littleton, CO).

    Techniques: Titration, Enzyme-linked Immunosorbent Assay, Western Blot, Immunoprecipitation, Cycling Probe Technology