α tubulin  (Novus Biologicals)

 
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    Name:
    alpha Tubulin Antibody 2D2
    Description:
    The alpha Tubulin Antibody 2D2 from Novus Biologicals is a mouse monoclonal antibody to alpha Tubulin This antibody reacts with human The alpha Tubulin Antibody 2D2 has been validated for the following applications Western Blot ELISA Immunocytochemistry Immunofluorescence
    Catalog Number:
    H00007846-M06
    Price:
    379
    Category:
    Primary Antibodies
    Purity:
    IgG purified
    Conjugate:
    Unconjugated
    Immunogen:
    TUBA1A (NP_006000 352 a.a. - 451 a.a.) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. KVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
    Size:
    0 1 mg
    Host:
    Mouse
    Isotype:
    IgG2a Kappa
    Buy from Supplier


    Structured Review

    Novus Biologicals α tubulin
    Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and <t>α-tubulin.</t> Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p
    The alpha Tubulin Antibody 2D2 from Novus Biologicals is a mouse monoclonal antibody to alpha Tubulin This antibody reacts with human The alpha Tubulin Antibody 2D2 has been validated for the following applications Western Blot ELISA Immunocytochemistry Immunofluorescence
    https://www.bioz.com/result/α tubulin/product/Novus Biologicals
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α tubulin - by Bioz Stars, 2021-07
    93/100 stars

    Images

    1) Product Images from "Lovastatin causes FaDu hypopharyngeal carcinoma cell death via AMPK-p63-survivin signaling cascade"

    Article Title: Lovastatin causes FaDu hypopharyngeal carcinoma cell death via AMPK-p63-survivin signaling cascade

    Journal: Scientific Reports

    doi: 10.1038/srep25082

    Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and α-tubulin. Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p
    Figure Legend Snippet: Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and α-tubulin. Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Transfection, MTT Assay, Flow Cytometry

    2) Product Images from "Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)"

    Article Title: Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)

    Journal: Frontiers in Plant Science

    doi: 10.3389/fpls.2015.00937

    Median longitudinal sections of soybean root apices treated with Cd indicating fluorescence signal strength, mitotic activity, and cortical MTs structure . The sections were double-labeled with anti-α-tubulin antibody (B-5-1-2) and DNA-binding dye (propidium iodide). An overview of untreated control roots (A,D,G) and the roots of seedlings treated with 85 μM (B,E,H) or 170 μM Cd (C,F,I) . Exposure to Cd results in a differentiated MT immunofluorescence signal, a strong reduction in the number of proliferating cells (red arrows indicate cells in different stages of mitosis) and different stages of cortical MTs structure disorders in cells of cortex tissue (yellow arrows). Bar = 100 μm (A–F) , 10 μm (G–I) .
    Figure Legend Snippet: Median longitudinal sections of soybean root apices treated with Cd indicating fluorescence signal strength, mitotic activity, and cortical MTs structure . The sections were double-labeled with anti-α-tubulin antibody (B-5-1-2) and DNA-binding dye (propidium iodide). An overview of untreated control roots (A,D,G) and the roots of seedlings treated with 85 μM (B,E,H) or 170 μM Cd (C,F,I) . Exposure to Cd results in a differentiated MT immunofluorescence signal, a strong reduction in the number of proliferating cells (red arrows indicate cells in different stages of mitosis) and different stages of cortical MTs structure disorders in cells of cortex tissue (yellow arrows). Bar = 100 μm (A–F) , 10 μm (G–I) .

    Techniques Used: Fluorescence, Activity Assay, Labeling, Binding Assay, Immunofluorescence

    Representative immunoblots probed with different antibodies against α-tubulin (A,B) and β-tubulin isoforms (C) . Individual tubulin isoforms are denoted by arrows marked α1–α6 for α-tubulin and β1–β4 for β-tubulin. The quantitative results for α-tubulin (antibody B-5-1-2) were calculated as a ratio of pixel intensity values to area of spots and data were presented considering the control as a reference point (100%). The values represent the average of three independent measurements with a standard deviation.
    Figure Legend Snippet: Representative immunoblots probed with different antibodies against α-tubulin (A,B) and β-tubulin isoforms (C) . Individual tubulin isoforms are denoted by arrows marked α1–α6 for α-tubulin and β1–β4 for β-tubulin. The quantitative results for α-tubulin (antibody B-5-1-2) were calculated as a ratio of pixel intensity values to area of spots and data were presented considering the control as a reference point (100%). The values represent the average of three independent measurements with a standard deviation.

    Techniques Used: Western Blot, Standard Deviation

    Relative expression of gene encoding α-tubulin isotypes . Fold change evaluated through real time PCR after moderate (85 μM Cd) and high (170 μM Cd) metal treatment. Values shown in the histogram are represented as a log 2 fold change compared to the control sample average of 0 (untreated seedlings). The results represent the mean (+SE) of three separate experiments.
    Figure Legend Snippet: Relative expression of gene encoding α-tubulin isotypes . Fold change evaluated through real time PCR after moderate (85 μM Cd) and high (170 μM Cd) metal treatment. Values shown in the histogram are represented as a log 2 fold change compared to the control sample average of 0 (untreated seedlings). The results represent the mean (+SE) of three separate experiments.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    Representative immunoblots probed with a set of different antibodies against tyrosinated α-tubulin (A) , detyrosinated α-tubulin (B) , acetylated α-tubulin (C) and polyglutamylated proteins (D) . Individual tubulin isoforms (spots) are denoted by arrows marked: αT1–αT11 (tyrosinated isoforms), αG1–αG10 (detyrosinated isoforms), αA1–αA9 (acetylated isoforms) and I–XIV (polyglutamylated proteins). The quantitative results were calculated as a ratio of pixel intensity values to the area of spots, and the data were presented considering the control or 170 μM Cd as a reference point (100%). Values represent the average of three independent measurements with a standard deviation.
    Figure Legend Snippet: Representative immunoblots probed with a set of different antibodies against tyrosinated α-tubulin (A) , detyrosinated α-tubulin (B) , acetylated α-tubulin (C) and polyglutamylated proteins (D) . Individual tubulin isoforms (spots) are denoted by arrows marked: αT1–αT11 (tyrosinated isoforms), αG1–αG10 (detyrosinated isoforms), αA1–αA9 (acetylated isoforms) and I–XIV (polyglutamylated proteins). The quantitative results were calculated as a ratio of pixel intensity values to the area of spots, and the data were presented considering the control or 170 μM Cd as a reference point (100%). Values represent the average of three independent measurements with a standard deviation.

    Techniques Used: Western Blot, Standard Deviation

    3) Product Images from "Nonsense-mediated decay factors are involved in the regulation of selenoprotein mRNA levels during selenium deficiency"

    Article Title: Nonsense-mediated decay factors are involved in the regulation of selenoprotein mRNA levels during selenium deficiency

    Journal: RNA

    doi: 10.1261/rna.043463.113

    SMG1 knockdown in HEK293T cells. ( A ) Western blot of SMG1 protein after knockdown with SMG1 siRNA or nonspecific control siRNA. α-Tubulin was used as a loading control. ( B ) Quantitation of A . Error bars represent standard deviation of the mean;
    Figure Legend Snippet: SMG1 knockdown in HEK293T cells. ( A ) Western blot of SMG1 protein after knockdown with SMG1 siRNA or nonspecific control siRNA. α-Tubulin was used as a loading control. ( B ) Quantitation of A . Error bars represent standard deviation of the mean;

    Techniques Used: Western Blot, Quantitation Assay, Standard Deviation

    4) Product Images from "Disruption of the Selenocysteine Lyase-Mediated Selenium Recycling Pathway Leads to Metabolic Syndrome in Mice"

    Article Title: Disruption of the Selenocysteine Lyase-Mediated Selenium Recycling Pathway Leads to Metabolic Syndrome in Mice

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.00293-12

    Selenoprotein profile in the liver of Scly KO mice fed an adequate Se diet. (A) Expression of selenoproteins SelS, SelK, TrxR1, SelW, GPx1, and SPS2 in Scly KO mice measured by Western blotting and normalized to the β-actin or α-tubulin
    Figure Legend Snippet: Selenoprotein profile in the liver of Scly KO mice fed an adequate Se diet. (A) Expression of selenoproteins SelS, SelK, TrxR1, SelW, GPx1, and SPS2 in Scly KO mice measured by Western blotting and normalized to the β-actin or α-tubulin

    Techniques Used: Mouse Assay, Expressing, Western Blot

    Related Articles

    other:

    Article Title: Diet-Induced Obesity in the Selenocysteine Lyase Knockout Mouse
    Article Snippet: Mouse GPx1, GPx3 (R & D Systems), SOCS3, SR-B1, UCP1 (Abcam), ACC1, AMPKalpha, pAMPKalpha, Pdh (Cell Signaling), SPS2 (Rockland, Inc.), Pcx, alpha-tubulin, TrxR1 (Novus Biologicals), Seps1, and beta-actin (Sigma-Aldrich) antibodies were diluted according to the manufacturer's protocols.

    Electrophoresis:

    Article Title: Nonsense-mediated decay factors are involved in the regulation of selenoprotein mRNA levels during selenium deficiency
    Article Snippet: Protein extracted using the preceding method was added to reduced Laemmli buffer (Bio-Rad), boiled for 5 min, and loaded into 4%–20% gradient polyacrylamide gels (Bio-Rad). .. Following electrophoresis, gel contents were transferred to a PVDF membrane (Millipore) and blocked with Odyssey blocking buffer (Li-Cor Biosciences) for 30 min. Membranes were then probed for proteins with the following primary antibodies: SMG1 (Dilution: 1:500; A300-394A, Bethyl Laboratories, Inc.) UPF1 (dilution: 1:1000; anti-RENT1, A301-902A, Bethyl Laboratories, Inc.), Grb2 (dilution: 1:1000; Upstate Cell Signaling), α-Tubulin (1:10,000; Novus Biologicals); and with the following secondary antibodies: goat anti-rabbit IRDye 680 (dilution: 1:10,000, Li-Cor Biosciences), goat anti-mouse IRDye 680 (dilution: 1:10,000, Li-Cor Biosciences), goat anti-mouse IRDye 800 (dilution: 1:10,000, Li-Cor Biosciences). .. All protein quantification was carried out using Odyssey's Image Studio version 3.0 (Li-Cor Biosciences).

    Blocking Assay:

    Article Title: Nonsense-mediated decay factors are involved in the regulation of selenoprotein mRNA levels during selenium deficiency
    Article Snippet: Protein extracted using the preceding method was added to reduced Laemmli buffer (Bio-Rad), boiled for 5 min, and loaded into 4%–20% gradient polyacrylamide gels (Bio-Rad). .. Following electrophoresis, gel contents were transferred to a PVDF membrane (Millipore) and blocked with Odyssey blocking buffer (Li-Cor Biosciences) for 30 min. Membranes were then probed for proteins with the following primary antibodies: SMG1 (Dilution: 1:500; A300-394A, Bethyl Laboratories, Inc.) UPF1 (dilution: 1:1000; anti-RENT1, A301-902A, Bethyl Laboratories, Inc.), Grb2 (dilution: 1:1000; Upstate Cell Signaling), α-Tubulin (1:10,000; Novus Biologicals); and with the following secondary antibodies: goat anti-rabbit IRDye 680 (dilution: 1:10,000, Li-Cor Biosciences), goat anti-mouse IRDye 680 (dilution: 1:10,000, Li-Cor Biosciences), goat anti-mouse IRDye 800 (dilution: 1:10,000, Li-Cor Biosciences). .. All protein quantification was carried out using Odyssey's Image Studio version 3.0 (Li-Cor Biosciences).

    Article Title: CD38 as a PET Imaging Target in Lung Cancer
    Article Snippet: 40 μ g of total protein was loaded into each well of a 4–12% Bolt Bis-Tris Plus gel (ThermoFisher Scientific). .. After proteins were transferred to a nitrocellulose membrane using the iBlot 2 (ThermoFisher Scientific), the membrane was blocked with Odyssey blocking buffer (LI-COR Biosciences), and incubated with anti-CD38 (1:1500) and anti- α -tubulin (1:2000) primary antibodies from Novus Biologicals overnight at 4 °C. .. The membrane was washed three times with PBST (phosphate buffered saline with 0.1% Tween 20), and incubated with the secondary antibodies donkey-anti-mouse DyLight 800 and donkey-anti-rabbit Dy-Light 680 (LI-COR Biosciences).

    Incubation:

    Article Title: CD38 as a PET Imaging Target in Lung Cancer
    Article Snippet: 40 μ g of total protein was loaded into each well of a 4–12% Bolt Bis-Tris Plus gel (ThermoFisher Scientific). .. After proteins were transferred to a nitrocellulose membrane using the iBlot 2 (ThermoFisher Scientific), the membrane was blocked with Odyssey blocking buffer (LI-COR Biosciences), and incubated with anti-CD38 (1:1500) and anti- α -tubulin (1:2000) primary antibodies from Novus Biologicals overnight at 4 °C. .. The membrane was washed three times with PBST (phosphate buffered saline with 0.1% Tween 20), and incubated with the secondary antibodies donkey-anti-mouse DyLight 800 and donkey-anti-rabbit Dy-Light 680 (LI-COR Biosciences).

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  • 93
    Novus Biologicals α tubulin
    Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and <t>α-tubulin.</t> Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p
    α 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/α tubulin/product/Novus Biologicals
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α tubulin - by Bioz Stars, 2021-07
    93/100 stars
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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
    Price from $9.99 to $1999.99
    β tubulin - by Bioz Stars, 2021-07
    93/100 stars
      Buy from Supplier

    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
    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, 2021-07
    91/100 stars
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    N/A
    The alpha Tubulin Antibody from Novus Biologicals is a rabbit polyclonal antibody to alpha Tubulin This antibody reacts with human mouse rat The alpha Tubulin Antibody has been validated for
      Buy from Supplier

    Image Search Results


    Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and α-tubulin. Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p

    Journal: Scientific Reports

    Article Title: Lovastatin causes FaDu hypopharyngeal carcinoma cell death via AMPK-p63-survivin signaling cascade

    doi: 10.1038/srep25082

    Figure Lengend Snippet: Lovastatin modulated p21 cip/Waf1 , survivin and cyclin D1 levels in FaDu cells. After 24 h treatment with indicated concentrations of lovastatin, the extent of p21 cip/Waf1 ( a ), cycin D1 ( b ) and survivin ( c ) were assessed by immunoblotting. Compiled results represent the mean ± S.E.M. of at least six independent experiments ( d ) After 6 h treatment with indicated concentrations of lovastatin, RT-PCR analysis was used to determine the extent of survivin mRNA . Compiled results are shown at the bottom (n = 4). ( e ) After transfection, immunoblotting was used to determine the extent of survivin and α-tubulin. Results shown are representative of four independent experiments. ( f ) MTT assay was used to determine cell viability after transfection. Compiled results are shown at the bottom (n = 4). ( g ) Flow cytometric analysis was used to detect cell apoptosis after transfection. Typical pattern shown are representative of four independent experiments. * p

    Article Snippet: Antibodies against p40 (p63 delta) and α-tubulin were obtained from Novus Biologicals (Littleton, CO, USA).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Transfection, MTT Assay, Flow Cytometry

    Median longitudinal sections of soybean root apices treated with Cd indicating fluorescence signal strength, mitotic activity, and cortical MTs structure . The sections were double-labeled with anti-α-tubulin antibody (B-5-1-2) and DNA-binding dye (propidium iodide). An overview of untreated control roots (A,D,G) and the roots of seedlings treated with 85 μM (B,E,H) or 170 μM Cd (C,F,I) . Exposure to Cd results in a differentiated MT immunofluorescence signal, a strong reduction in the number of proliferating cells (red arrows indicate cells in different stages of mitosis) and different stages of cortical MTs structure disorders in cells of cortex tissue (yellow arrows). Bar = 100 μm (A–F) , 10 μm (G–I) .

    Journal: Frontiers in Plant Science

    Article Title: Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)

    doi: 10.3389/fpls.2015.00937

    Figure Lengend Snippet: Median longitudinal sections of soybean root apices treated with Cd indicating fluorescence signal strength, mitotic activity, and cortical MTs structure . The sections were double-labeled with anti-α-tubulin antibody (B-5-1-2) and DNA-binding dye (propidium iodide). An overview of untreated control roots (A,D,G) and the roots of seedlings treated with 85 μM (B,E,H) or 170 μM Cd (C,F,I) . Exposure to Cd results in a differentiated MT immunofluorescence signal, a strong reduction in the number of proliferating cells (red arrows indicate cells in different stages of mitosis) and different stages of cortical MTs structure disorders in cells of cortex tissue (yellow arrows). Bar = 100 μm (A–F) , 10 μm (G–I) .

    Article Snippet: Antibodies The following antibodies were used in the detection of tubulin subunits: mouse monoclonal antibody B-5-1-2 (IgG1; Sigma T5168; diluted 1:5,000) was used to recognize an epitope located in the C-terminal end of the α-tubulin isoforms; mouse monoclonal antibody TU-01 (IgG1; Novus Biologicals NB500-333; diluted 1:2,000) was directed against the N-terminal structural domain (epitope aa 65–97) of the α-tubulin; and mouse monoclonal antibody TU-06 (IgM; Novus Biologicals NB120-7792; diluted 1:2,000) was directed against the N-terminal structural domain of β-tubulin and reacted with all charge variants of tubulin.

    Techniques: Fluorescence, Activity Assay, Labeling, Binding Assay, Immunofluorescence

    Representative immunoblots probed with different antibodies against α-tubulin (A,B) and β-tubulin isoforms (C) . Individual tubulin isoforms are denoted by arrows marked α1–α6 for α-tubulin and β1–β4 for β-tubulin. The quantitative results for α-tubulin (antibody B-5-1-2) were calculated as a ratio of pixel intensity values to area of spots and data were presented considering the control as a reference point (100%). The values represent the average of three independent measurements with a standard deviation.

    Journal: Frontiers in Plant Science

    Article Title: Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)

    doi: 10.3389/fpls.2015.00937

    Figure Lengend Snippet: Representative immunoblots probed with different antibodies against α-tubulin (A,B) and β-tubulin isoforms (C) . Individual tubulin isoforms are denoted by arrows marked α1–α6 for α-tubulin and β1–β4 for β-tubulin. The quantitative results for α-tubulin (antibody B-5-1-2) were calculated as a ratio of pixel intensity values to area of spots and data were presented considering the control as a reference point (100%). The values represent the average of three independent measurements with a standard deviation.

    Article Snippet: Antibodies The following antibodies were used in the detection of tubulin subunits: mouse monoclonal antibody B-5-1-2 (IgG1; Sigma T5168; diluted 1:5,000) was used to recognize an epitope located in the C-terminal end of the α-tubulin isoforms; mouse monoclonal antibody TU-01 (IgG1; Novus Biologicals NB500-333; diluted 1:2,000) was directed against the N-terminal structural domain (epitope aa 65–97) of the α-tubulin; and mouse monoclonal antibody TU-06 (IgM; Novus Biologicals NB120-7792; diluted 1:2,000) was directed against the N-terminal structural domain of β-tubulin and reacted with all charge variants of tubulin.

    Techniques: Western Blot, Standard Deviation

    Relative expression of gene encoding α-tubulin isotypes . Fold change evaluated through real time PCR after moderate (85 μM Cd) and high (170 μM Cd) metal treatment. Values shown in the histogram are represented as a log 2 fold change compared to the control sample average of 0 (untreated seedlings). The results represent the mean (+SE) of three separate experiments.

    Journal: Frontiers in Plant Science

    Article Title: Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)

    doi: 10.3389/fpls.2015.00937

    Figure Lengend Snippet: Relative expression of gene encoding α-tubulin isotypes . Fold change evaluated through real time PCR after moderate (85 μM Cd) and high (170 μM Cd) metal treatment. Values shown in the histogram are represented as a log 2 fold change compared to the control sample average of 0 (untreated seedlings). The results represent the mean (+SE) of three separate experiments.

    Article Snippet: Antibodies The following antibodies were used in the detection of tubulin subunits: mouse monoclonal antibody B-5-1-2 (IgG1; Sigma T5168; diluted 1:5,000) was used to recognize an epitope located in the C-terminal end of the α-tubulin isoforms; mouse monoclonal antibody TU-01 (IgG1; Novus Biologicals NB500-333; diluted 1:2,000) was directed against the N-terminal structural domain (epitope aa 65–97) of the α-tubulin; and mouse monoclonal antibody TU-06 (IgM; Novus Biologicals NB120-7792; diluted 1:2,000) was directed against the N-terminal structural domain of β-tubulin and reacted with all charge variants of tubulin.

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Representative immunoblots probed with a set of different antibodies against tyrosinated α-tubulin (A) , detyrosinated α-tubulin (B) , acetylated α-tubulin (C) and polyglutamylated proteins (D) . Individual tubulin isoforms (spots) are denoted by arrows marked: αT1–αT11 (tyrosinated isoforms), αG1–αG10 (detyrosinated isoforms), αA1–αA9 (acetylated isoforms) and I–XIV (polyglutamylated proteins). The quantitative results were calculated as a ratio of pixel intensity values to the area of spots, and the data were presented considering the control or 170 μM Cd as a reference point (100%). Values represent the average of three independent measurements with a standard deviation.

    Journal: Frontiers in Plant Science

    Article Title: Cadmium affects microtubule organization and post-translational modifications of tubulin in seedlings of soybean (Glycine max L.)

    doi: 10.3389/fpls.2015.00937

    Figure Lengend Snippet: Representative immunoblots probed with a set of different antibodies against tyrosinated α-tubulin (A) , detyrosinated α-tubulin (B) , acetylated α-tubulin (C) and polyglutamylated proteins (D) . Individual tubulin isoforms (spots) are denoted by arrows marked: αT1–αT11 (tyrosinated isoforms), αG1–αG10 (detyrosinated isoforms), αA1–αA9 (acetylated isoforms) and I–XIV (polyglutamylated proteins). The quantitative results were calculated as a ratio of pixel intensity values to the area of spots, and the data were presented considering the control or 170 μM Cd as a reference point (100%). Values represent the average of three independent measurements with a standard deviation.

    Article Snippet: Antibodies The following antibodies were used in the detection of tubulin subunits: mouse monoclonal antibody B-5-1-2 (IgG1; Sigma T5168; diluted 1:5,000) was used to recognize an epitope located in the C-terminal end of the α-tubulin isoforms; mouse monoclonal antibody TU-01 (IgG1; Novus Biologicals NB500-333; diluted 1:2,000) was directed against the N-terminal structural domain (epitope aa 65–97) of the α-tubulin; and mouse monoclonal antibody TU-06 (IgM; Novus Biologicals NB120-7792; diluted 1:2,000) was directed against the N-terminal structural domain of β-tubulin and reacted with all charge variants of tubulin.

    Techniques: Western Blot, Standard Deviation

    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