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tuba αtubulin  (Proteintech)


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    Proteintech tuba αtubulin
    Tuba αtubulin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 3477 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tuba/alpha+Tubulin+Antibody/pm42529830-488-42-48
    Average 96 stars, based on 3477 article reviews
    tuba αtubulin - by Bioz Stars, 2026-11
    96/100 stars

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    Produced:

    Article Title: The non-redundant functions of PIWI family proteins in gametogenesis in golden hamsters.
    Article Snippet: Protein expression was measured by chemiluminescence and quantified as an area under the curve using the Compass for Simple Western program (ProteinSimple). .. Proteins were detectedwith the following primary antibodies: PIWIL1 (1:100; GL Biochem, China); PIWIL2 (1:100; Millipore, #MABE363); TUBA (1:200; Proteintech, #66031-1-Ig); PIWIL3 (1:100, lab produced) and PIWIL4 (1:100, lab produced); Beta Actin (1:200, Proteintech, #66009-1-Ig). .. Testes and ovaries were fixed in Bouin’s fixative (Sigma-Aldrich, MBD1105) overnight at 4 °C, embedded in paraffin, and sectioned at 5μm.

    other:

    Article Title: Glutamine sensing licenses cholesterol synthesis.
    Article Snippet: The mevalonate pathway produces essential lipid metabolites such as cholesterol.. Although this pathway is negatively regulated by metabolic intermediates, little is known of the metabolites that positively regulate its activity.. We found that the amino acid glutamine is required to activate the mevalonate pathway.



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    Secretion of ER-generated HA-Ub E when SP-HA-Ub is expressed in HEK293T cells. (A) Schematic representation of HA-Ub, SP-HA-Ub, and LCN2. The 20-amino-acid signal peptide (SP) originated from LCN2 was added to the N-terminus of HA-Ub. (B) Altered fate of SP-HA-Ub due to the recognition of SP by SRP. (C) SP-HA-Ub or HA-Ub construct transfected into HEK293T cells and Ub n (free Ub and Ub conjugates) and HA bands detected by immunoblotting using HEK293T cell lysates and the culture medium. For better detection of HA bands, the immunoblot with a long exposure time is also shown for SP-HA-Ub (long: 2 min; short: 7 sec). <t>α-Tubulin</t> (α-Tub) or Coomassie blue staining was used as a loading control.
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    Secretion of ER-generated HA-Ub E when SP-HA-Ub is expressed in HEK293T cells. (A) Schematic representation of HA-Ub, SP-HA-Ub, and LCN2. The 20-amino-acid signal peptide (SP) originated from LCN2 was added to the N-terminus of HA-Ub. (B) Altered fate of SP-HA-Ub due to the recognition of SP by SRP. (C) SP-HA-Ub or HA-Ub construct transfected into HEK293T cells and Ub n (free Ub and Ub conjugates) and HA bands detected by immunoblotting using HEK293T cell lysates and the culture medium. For better detection of HA bands, the immunoblot with a long exposure time is also shown for SP-HA-Ub (long: 2 min; short: 7 sec). <t>α-Tubulin</t> (α-Tub) or Coomassie blue staining was used as a loading control.
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    Secretion of ER-generated HA-Ub E when SP-HA-Ub is expressed in HEK293T cells. (A) Schematic representation of HA-Ub, SP-HA-Ub, and LCN2. The 20-amino-acid signal peptide (SP) originated from LCN2 was added to the N-terminus of HA-Ub. (B) Altered fate of SP-HA-Ub due to the recognition of SP by SRP. (C) SP-HA-Ub or HA-Ub construct transfected into HEK293T cells and Ub n (free Ub and Ub conjugates) and HA bands detected by immunoblotting using HEK293T cell lysates and the culture medium. For better detection of HA bands, the immunoblot with a long exposure time is also shown for SP-HA-Ub (long: 2 min; short: 7 sec). <t>α-Tubulin</t> (α-Tub) or Coomassie blue staining was used as a loading control.
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    ( A ) Immunoblot (IB) analyses of WT and eIF2α S51A AN3–12 cells that were uninfected (uninf), infected with Toxoplasma ( Toxo ), or tunicamycin (TUN)-treated (3 μg/ml) for 24 hours <t>(h):</t> <t>ATF4;</t> phospho-EIF2α (Ser51), ~38 kDa; α-Tubulin <t>(TUBA),</t> ~55 kDa; and TgGAP45. ( B ) Heatmap of mRNA levels of ATF4 target genes in uninf, Toxo , and TUN (3 μg/ml)-treated ES-2 cells; n=3 independent cultures. ( C and D ) WT and ATF4 KO ES-2 cells were uninf or Toxo for 24 h and analyzed by qPCR for SHMT2 and MTHFD2 . Transcripts were normalized to ACTB and are relative to WT uninf. Data are mean ± SD of n=7 independent cultures. *p<0.05; ****p<0.0001 for uninf versus Toxo by two-way ANOVA analysis. ( E ) IB of ES-2 cells as indicated: MTHFD2, ~32 kDa and TUBA. ( F, G and H ) ES-2 cells as indicated were analyzed for mtDNA by qPCR for DLOOP , mt -ND1 and mt -CTYB normalized to RUNX2 levels and relative to WT uninfected. Data are mean ± SD of n=4 independent cultures. *p<0.05; **p<0.01 for uninf versus Toxo , and #p<0.05; ##p<0.01 for WT versus MTHFD2 KO by two-way ANOVA analysis. ( I ) IB analysis of ES-2 cells as indicated at 24 hpi (MOI: 4 for Toxo ): ATF4, VCL, and TgGAP45. ( J and K) Cells treated as in ( I ) were analyzed by qPCR as in ( C and D ). Data are mean ± SD of n=4 independent cultures, *p<0.05; **p<0.01 by one-way ANOVA analysis. ( L ) IB analysis of WT and HRI KO ES-2 cells that were uninf or Toxo at 24 hpi; Toxoplasma GRA7 (TgGRA7), ~32 kDa, ( M ) IB analysis of uninf and Toxo WT and OMA1 KO mouse embryonic fibroblasts (MEFs) at 24 hpi: OMA1, ~35 kDa, ATF4, ACTB, and TgGAP45. ( N ) Toxo WT and ATF4 KO ES-2 were treated ± ISRIB (200nM) and analyzed 24 hpi via flow cytometry for Toxoplasma burden (mCherry median FI). Data are mean ± SEM of n=3 biological experiments, **p< 0.01 for DMSO versus ISRIB, #### p < 0.0001 for WT versus ATF4 KO by two-way ANOVA analysis.
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    Image Search Results


    Secretion of ER-generated HA-Ub E when SP-HA-Ub is expressed in HEK293T cells. (A) Schematic representation of HA-Ub, SP-HA-Ub, and LCN2. The 20-amino-acid signal peptide (SP) originated from LCN2 was added to the N-terminus of HA-Ub. (B) Altered fate of SP-HA-Ub due to the recognition of SP by SRP. (C) SP-HA-Ub or HA-Ub construct transfected into HEK293T cells and Ub n (free Ub and Ub conjugates) and HA bands detected by immunoblotting using HEK293T cell lysates and the culture medium. For better detection of HA bands, the immunoblot with a long exposure time is also shown for SP-HA-Ub (long: 2 min; short: 7 sec). α-Tubulin (α-Tub) or Coomassie blue staining was used as a loading control.

    Journal: BMB Reports

    Article Title: Improved efficiency of protein aggregate removal using ubiquitin with a signal peptide

    doi: 10.5483/BMBRep.2025-0153

    Figure Lengend Snippet: Secretion of ER-generated HA-Ub E when SP-HA-Ub is expressed in HEK293T cells. (A) Schematic representation of HA-Ub, SP-HA-Ub, and LCN2. The 20-amino-acid signal peptide (SP) originated from LCN2 was added to the N-terminus of HA-Ub. (B) Altered fate of SP-HA-Ub due to the recognition of SP by SRP. (C) SP-HA-Ub or HA-Ub construct transfected into HEK293T cells and Ub n (free Ub and Ub conjugates) and HA bands detected by immunoblotting using HEK293T cell lysates and the culture medium. For better detection of HA bands, the immunoblot with a long exposure time is also shown for SP-HA-Ub (long: 2 min; short: 7 sec). α-Tubulin (α-Tub) or Coomassie blue staining was used as a loading control.

    Article Snippet: TUBA/α-Tubulin , Mouse IgG , Santa Cruz Biotechnology , SC-32293 , 1:1,000 , .

    Techniques: Generated, Construct, Transfection, Western Blot, Staining, Control

    Functional comparison between HA-Ub and HA-Ub E originating from SP-HA-Ub expressed in HEK293T cells. (A) Immunoblot detection of HA-Ub and HA-Ub E in HEK293T cells treated with 1 μM bortezomib (BTZ) or 100 nM bafilomycin A1 (BAF A1) for 18 h. Ub n and HA bands were assessed in cell lysates and cultured media. α-Tubulin (α-Tub) or Coomassie blue staining was used as a loading control. (B) Quantification of HA (HA-Ub and HA-Ub E conjugates) band intensities in (A) normalized to α-tubulin levels. Normalized HA band intensities were expressed as fold changes relative to non-treated controls (–; SP-HA-Ub or HA-Ub, n = 3 per group). Data are presented as the mean ± SEM from the indicated number of samples using the two-tailed unpaired t-test. # P < 0.1; *P < 0.05; **P < 0.01 vs. each non-treated control.

    Journal: BMB Reports

    Article Title: Improved efficiency of protein aggregate removal using ubiquitin with a signal peptide

    doi: 10.5483/BMBRep.2025-0153

    Figure Lengend Snippet: Functional comparison between HA-Ub and HA-Ub E originating from SP-HA-Ub expressed in HEK293T cells. (A) Immunoblot detection of HA-Ub and HA-Ub E in HEK293T cells treated with 1 μM bortezomib (BTZ) or 100 nM bafilomycin A1 (BAF A1) for 18 h. Ub n and HA bands were assessed in cell lysates and cultured media. α-Tubulin (α-Tub) or Coomassie blue staining was used as a loading control. (B) Quantification of HA (HA-Ub and HA-Ub E conjugates) band intensities in (A) normalized to α-tubulin levels. Normalized HA band intensities were expressed as fold changes relative to non-treated controls (–; SP-HA-Ub or HA-Ub, n = 3 per group). Data are presented as the mean ± SEM from the indicated number of samples using the two-tailed unpaired t-test. # P < 0.1; *P < 0.05; **P < 0.01 vs. each non-treated control.

    Article Snippet: TUBA/α-Tubulin , Mouse IgG , Santa Cruz Biotechnology , SC-32293 , 1:1,000 , .

    Techniques: Functional Assay, Comparison, Western Blot, Cell Culture, Staining, Control, Two Tailed Test

    Improved protein aggregate removal capability by autophagy under proteotoxic stress conditions when SP-HA-Ub is expressed in HEK293T cells. (A) Immunoblot detection of HA-Ub and HA-Ub E in HEK293T cells treated with 20 nM NaAsO 2 in the presence or absence of 2 μM torin 1 for 18 h. Ubn and HA bands were assessed in cell lysates. For better detection of HA bands, the immunoblot with a long exposure time was also shown for SP-HA-Ub (long: 5 min; short: 3 sec). α-Tubulin (α-Tub) was used as a loading control. (B) Quantification of HA (HA-Ub and HA-Ub E conjugates) band intensities in (A) normalized to α-tubulin levels. Normalized HA band intensities expressed as fold changes relative to non-treated controls (–; HA-Ub, n = 3, and SP-HA-Ub, n = 7). Data are presented as the mean ± SEM from the indicated number of samples using the two-tailed unpaired t-test. **P < 0.01 vs. each non-treated control; ns, not significant.

    Journal: BMB Reports

    Article Title: Improved efficiency of protein aggregate removal using ubiquitin with a signal peptide

    doi: 10.5483/BMBRep.2025-0153

    Figure Lengend Snippet: Improved protein aggregate removal capability by autophagy under proteotoxic stress conditions when SP-HA-Ub is expressed in HEK293T cells. (A) Immunoblot detection of HA-Ub and HA-Ub E in HEK293T cells treated with 20 nM NaAsO 2 in the presence or absence of 2 μM torin 1 for 18 h. Ubn and HA bands were assessed in cell lysates. For better detection of HA bands, the immunoblot with a long exposure time was also shown for SP-HA-Ub (long: 5 min; short: 3 sec). α-Tubulin (α-Tub) was used as a loading control. (B) Quantification of HA (HA-Ub and HA-Ub E conjugates) band intensities in (A) normalized to α-tubulin levels. Normalized HA band intensities expressed as fold changes relative to non-treated controls (–; HA-Ub, n = 3, and SP-HA-Ub, n = 7). Data are presented as the mean ± SEM from the indicated number of samples using the two-tailed unpaired t-test. **P < 0.01 vs. each non-treated control; ns, not significant.

    Article Snippet: TUBA/α-Tubulin , Mouse IgG , Santa Cruz Biotechnology , SC-32293 , 1:1,000 , .

    Techniques: Western Blot, Control, Two Tailed Test

    ( A ) Immunoblot (IB) analyses of WT and eIF2α S51A AN3–12 cells that were uninfected (uninf), infected with Toxoplasma ( Toxo ), or tunicamycin (TUN)-treated (3 μg/ml) for 24 hours (h): ATF4; phospho-EIF2α (Ser51), ~38 kDa; α-Tubulin (TUBA), ~55 kDa; and TgGAP45. ( B ) Heatmap of mRNA levels of ATF4 target genes in uninf, Toxo , and TUN (3 μg/ml)-treated ES-2 cells; n=3 independent cultures. ( C and D ) WT and ATF4 KO ES-2 cells were uninf or Toxo for 24 h and analyzed by qPCR for SHMT2 and MTHFD2 . Transcripts were normalized to ACTB and are relative to WT uninf. Data are mean ± SD of n=7 independent cultures. *p<0.05; ****p<0.0001 for uninf versus Toxo by two-way ANOVA analysis. ( E ) IB of ES-2 cells as indicated: MTHFD2, ~32 kDa and TUBA. ( F, G and H ) ES-2 cells as indicated were analyzed for mtDNA by qPCR for DLOOP , mt -ND1 and mt -CTYB normalized to RUNX2 levels and relative to WT uninfected. Data are mean ± SD of n=4 independent cultures. *p<0.05; **p<0.01 for uninf versus Toxo , and #p<0.05; ##p<0.01 for WT versus MTHFD2 KO by two-way ANOVA analysis. ( I ) IB analysis of ES-2 cells as indicated at 24 hpi (MOI: 4 for Toxo ): ATF4, VCL, and TgGAP45. ( J and K) Cells treated as in ( I ) were analyzed by qPCR as in ( C and D ). Data are mean ± SD of n=4 independent cultures, *p<0.05; **p<0.01 by one-way ANOVA analysis. ( L ) IB analysis of WT and HRI KO ES-2 cells that were uninf or Toxo at 24 hpi; Toxoplasma GRA7 (TgGRA7), ~32 kDa, ( M ) IB analysis of uninf and Toxo WT and OMA1 KO mouse embryonic fibroblasts (MEFs) at 24 hpi: OMA1, ~35 kDa, ATF4, ACTB, and TgGAP45. ( N ) Toxo WT and ATF4 KO ES-2 were treated ± ISRIB (200nM) and analyzed 24 hpi via flow cytometry for Toxoplasma burden (mCherry median FI). Data are mean ± SEM of n=3 biological experiments, **p< 0.01 for DMSO versus ISRIB, #### p < 0.0001 for WT versus ATF4 KO by two-way ANOVA analysis.

    Journal: Science (New York, N.Y.)

    Article Title: Mitochondria protect against an intracellular pathogen by restricting access to folate

    doi: 10.1126/science.adr6326

    Figure Lengend Snippet: ( A ) Immunoblot (IB) analyses of WT and eIF2α S51A AN3–12 cells that were uninfected (uninf), infected with Toxoplasma ( Toxo ), or tunicamycin (TUN)-treated (3 μg/ml) for 24 hours (h): ATF4; phospho-EIF2α (Ser51), ~38 kDa; α-Tubulin (TUBA), ~55 kDa; and TgGAP45. ( B ) Heatmap of mRNA levels of ATF4 target genes in uninf, Toxo , and TUN (3 μg/ml)-treated ES-2 cells; n=3 independent cultures. ( C and D ) WT and ATF4 KO ES-2 cells were uninf or Toxo for 24 h and analyzed by qPCR for SHMT2 and MTHFD2 . Transcripts were normalized to ACTB and are relative to WT uninf. Data are mean ± SD of n=7 independent cultures. *p<0.05; ****p<0.0001 for uninf versus Toxo by two-way ANOVA analysis. ( E ) IB of ES-2 cells as indicated: MTHFD2, ~32 kDa and TUBA. ( F, G and H ) ES-2 cells as indicated were analyzed for mtDNA by qPCR for DLOOP , mt -ND1 and mt -CTYB normalized to RUNX2 levels and relative to WT uninfected. Data are mean ± SD of n=4 independent cultures. *p<0.05; **p<0.01 for uninf versus Toxo , and #p<0.05; ##p<0.01 for WT versus MTHFD2 KO by two-way ANOVA analysis. ( I ) IB analysis of ES-2 cells as indicated at 24 hpi (MOI: 4 for Toxo ): ATF4, VCL, and TgGAP45. ( J and K) Cells treated as in ( I ) were analyzed by qPCR as in ( C and D ). Data are mean ± SD of n=4 independent cultures, *p<0.05; **p<0.01 by one-way ANOVA analysis. ( L ) IB analysis of WT and HRI KO ES-2 cells that were uninf or Toxo at 24 hpi; Toxoplasma GRA7 (TgGRA7), ~32 kDa, ( M ) IB analysis of uninf and Toxo WT and OMA1 KO mouse embryonic fibroblasts (MEFs) at 24 hpi: OMA1, ~35 kDa, ATF4, ACTB, and TgGAP45. ( N ) Toxo WT and ATF4 KO ES-2 were treated ± ISRIB (200nM) and analyzed 24 hpi via flow cytometry for Toxoplasma burden (mCherry median FI). Data are mean ± SEM of n=3 biological experiments, **p< 0.01 for DMSO versus ISRIB, #### p < 0.0001 for WT versus ATF4 KO by two-way ANOVA analysis.

    Article Snippet: The following antibodies were used: ATF4 (CST #11815), VCL (CST #4650), pS6K (CST #97596), TUBA (Proteintech 66031–1-Ig), MTHFD2 (CST #41377), SHMT2 (CST #33443), MTHFD1L (Invitrogen #PA5–100158), MTHFD1 (Sigma #HPA015006), phospho-eIF2a (Ser51) (CST #9721), ACTB (CST #4970), OMA1 (Santa Cruz #515788), BIP (CST #3183), ATF6 (CST #65880), c-Myc ( CST #18583), anti-DNA (EMD Millipore #CBL186), GCN2 (CST#3302); GCN2 (abcam ab134053), TgGra45 (Dr. D Soldati; U. of Geneva), TgMAF1 and TgGRA7 (Dr. J Boothroyd; Stanford University) antisera.

    Techniques: Western Blot, Infection, Flow Cytometry