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mouse monoclonal anti tubulin e7  (Developmental Studies Hybridoma Bank)


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    Developmental Studies Hybridoma Bank mouse monoclonal anti tubulin e7
    Mouse Monoclonal Anti Tubulin E7, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 97/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+e7+anti+tubulin+antibody/pmc13103552-4-0-8?v=Developmental+Studies+Hybridoma+Bank
    Average 97 stars, based on 29 article reviews
    mouse monoclonal anti tubulin e7 - by Bioz Stars, 2026-07
    97/100 stars

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    (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; <t>tubulin</t> was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.
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    Developmental Studies Hybridoma Bank mouse monoclonal anti β tubulin
    (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; <t>tubulin</t> was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.
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    Developmental Studies Hybridoma Bank mouse anti tubulin
    (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; <t>tubulin</t> was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.
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    Developmental Studies Hybridoma Bank mouse anti tubulinβ
    (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; <t>tubulin</t> was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.
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    (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; tubulin was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.

    Journal: bioRxiv

    Article Title: Scp160 deletion suppresses TDP-43 aggregation and toxicity in Saccharomyces cerevisiae

    doi: 10.64898/2026.04.28.721091

    Figure Lengend Snippet: (A) Ribosome sedimentation profiles of WT, scp160Δ , and bfr1Δ cells. Cells were grown in YPDA to mid-log phase and lysed under polysome-preserving conditions. Lysates were centrifuged through 15-45% sucrose gradients and fractionated with the continuous measurement of absorbance at 256 nm to visualize ribosomal species peaks. Positions of 40S and 60S ribosomal subunits, 80S monosomes, and polysomes are indicated. (B) Semi-quantitative immunoblot analysis of TDP43-GFP expression in WT, bfr1Δ , and scp160Δ cells carrying P GAL1 -TDP43-GFP. Cells were grown on raffinose and then shifted to either glucose-repressing conditions or to galactose for induction for 4 h. TDP43-GFP was detected with an anti-GFP antibody; tubulin was used as a loading control. (C) Immunoblot analysis of secretory-protein reporter Rny1-FLAG in WT, scp160Δ , and bfr1Δ cells. Rny1-FLAG (wild-type (wt) or the glycosylation-defective Rny1-FLAG W399R mutant) was expressed from the 2 m plasmid from the ADH promoter. Rny1-FLAG species were detected with anti-FLAG antibody. Tubulin was used as a loading control.

    Article Snippet: Monoclonal anti-GFP antibodies were from Santa Cruz Biotechnology (sc-9996) and used at 800 ng/mL; mouse monoclonal anti-α-tubulin antibodies (12G10) were obtained from the Developmental Studies Hybridoma Bank (DSHB; University of Iowa, Iowa City, IA, USA) and used at a 1:1000 dilution; mouse monoclonal anti-FLAG antibodies (M2) were purchased from Sigma and used at 1 μg/mL; anti-mouse IgG-HRP were from GE-Healthcare (NA931) and used at a dilution of 1:5000.

    Techniques: Sedimentation, Preserving, Western Blot, Expressing, Control, Glycoproteomics, Mutagenesis, Plasmid Preparation