Tata binding protein

Manufactured by Santa Cruz Biotechnology

Sourced in United States, United Kingdom

TATA-binding protein (TBP) is a core transcription factor that binds to the TATA box sequence in the promoter region of eukaryotic genes. TBP is a crucial component of the transcription initiation complex and plays a central role in the regulation of gene expression.

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Lab products found in correlation

Protease and phosphatase inhibitor, by Thermo Fisher Scientific (1 mentions) Acrylamide gel, by Bio-Rad (1 mentions) Immobilon forte western hrp substrate, by Merck Group (1 mentions) Tox tox2, by Cell Signaling Technology (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Gapdh, by Merck Group (1 mentions) Anti α sma antibody, by GeneTex (1 mentions) Immobilon p, by Merck Group (1 mentions) Snail1, by Santa Cruz Biotechnology (1 mentions) Anti vimentin antibody, by Merck Group (1 mentions) Nuclear extraction kit, by Active Motif (1 mentions) β catenin, by Santa Cruz Biotechnology (1 mentions) Rhifn γ, by Thermo Fisher Scientific (1 mentions) Cyclin d1, by Cell Signaling Technology (1 mentions) Rhigf 1, by Thermo Fisher Scientific (1 mentions) Rhil 6, by Thermo Fisher Scientific (1 mentions) Goat anti mouse igg horseradish peroxidase hrp, by Santa Cruz Biotechnology (1 mentions) Tannic acid c76h52o46, by Merck Group (1 mentions) β actin antibody, by Santa Cruz Biotechnology (1 mentions) Stat1, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

TATA box binding protein (Tbp), (2 citations) Anti-TATA box binding protein (TBP) (2 citations)

6 protocols using tata binding protein

Quantifying Activated mTOR Signaling in CD4+ T Cells

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CD4⁺ T cells (1 × 10⁶) were isolated from the lung tumors of CD4/ALK4-KO or WT mice. Cells were washed with PBS and harvested in lysis buffer supplemented with protease and phosphatase inhibitors (Invitrogen). Protein homogenates were loaded on acrylamide gels (Biorad), transferred onto a PVDF membrane (Millipore), blocked with 5% non-fat milk (or 5% BSA for phosphor-mTOR) at 25oC for 1 h, and probed with primary antibodies against phosphor-mTOR (Cell Signaling), TATA-binding protein (TBP) (Santa Cruz), Tox/Tox2 (Cell signaling) and GAPDH (Merck Millipore), at 4oC overnight. The blot was subsequently incubated with horseradish peroxidase-linked secondary antibodies at 25oC for 1 h, and developed using the Immobilon Forte Western HRP substrate (Merck Millipore).

Morianos I., Tsitsopoulou A., Potaris K., Valakos D., Fari O., Vatsellas G., Bostantzoglou C., Photiades A., Gaga M., Xanthou G, & Semitekolou M. (2021). Activin-A impedes the establishment of CD4+ T cell exhaustion and enhances anti-tumor immunity in the lung. Journal of Experimental & Clinical Cancer Research : CR, 40, 295.

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Western Blot Analysis of EMT Markers

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Cytosolic and nuclear extracts were obtained using an Active Motif nuclear extraction kit (Active Motif) according to the manufacturer’s instructions.
Cytosolic and nuclear extracts were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), transferred to polyvinylidene difluoride (PVDF) membrane sheets (Immobilon-P, Millipore) and probed with the required antibody diluted in 0.1% PBS-Tween with 5% nonfat dry milk. After 1 hr of incubation, the membranes were washed with 0.1% PBS-Tween and then were incubated for 1 hr with peroxidase-conjugated sheep anti-mouse or sheep anti-rabbit IgG antibody (Amersham International) diluted 1:3,000 in 0.1% PBS-Tween with 5% nonfat dry milk. The membranes were washed again with 0.1% PBS-Tween, and proteins were detected by enhanced chemiluminescence (Perkin Elmer).
Anti-E-cadherin, β-catenin, tubulin, SNAIL-1, and TATA-binding protein (TBP) antibodies were all provided by Santa Cruz Biotechnology, Inc. tubulin and TBP were used as loading controls for the cytosol and the nucleus, respectively. The anti-vimentin antibody was provided by Sigma Chemical Co. The anti-α-SMA antibody was from GeneTex. The anti-Smad2 and p-Smad2 antibodies were from Abcam.

Gulino G.R., Polimeni M., Prato M., Gazzano E., Kopecka J., Colombatto S., Ghigo D, & Aldieri E. (2015). Effects of Chrysotile Exposure in Human Bronchial Epithelial Cells: Insights into the Pathogenic Mechanisms of Asbestos-Related Diseases. Environmental Health Perspectives, 124(6), 776-784.

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Cytokine-Induced Signaling Pathway Inhibition

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Jak2, p‐Jak2 (Y1007/1008), p‐STAT1 (Y701), p‐STAT1 (S727), p‐STAT3 (Y705), p‐STAT3 (S727), Erk1/2, p‐Erk1/2 (Thr202/Tyr204), p38, p‐p38, p27^Kip and cyclin D1 antibodies were purchased from Cell Signaling Technologies (Beverly, MA, USA). STAT1, p21^Waf1/Cip1, cyclin E, p53, CDK‐4, STAT3, Bax, Bcl‐2, Bcl‐X_L, TATA binding protein (TBP), β‐actin antibodies and secondary antibody [rabbit, goat antimouse IgG‐horseradish peroxidase (HRP)] were obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA). The inhibitors of Jak2 (AG490), p38 (SB203580) and Erk1/2 (PD98059) were obtained from Sigma‐Aldrich (St. Louis, MO, USA). The inhibitor for TAK1 (5Z‐7‐oxozeaenol) was obtained from Millipore (Billerica, MA, USA). The inhibitors were dissolved in dimethyl sulphoxide (DMSO) for the experiments. Tannic acid (C₇₆H₅₂O₄₆) for the analysis is purchased from Sigma‐Aldrich and dissolved in water for the treatment. The rhIL‐6 and rhIFN‐γ were purchased from Peprotech (Rocky Hill, NJ, USA) and rhIGF‐1 were obtained from Invitrogen (MD, USA). Tamoxifen (TAM) is purchased from Sigma Chemicals (St. Louis, MO, USA) and dissolved in DMSO. Gefitinib (GEF) was purchased from Cell Signaling Technologies.

Darvin P., Joung Y.H., Kang D.Y., Sp N., Byun H.J., Hwang T.S., Sasidharakurup H., Lee C.H., Cho K.H., Park K.D., Lee H.K, & Yang Y.M. (2016). Tannic acid inhibits EGFR/STAT1/3 and enhances p38/STAT1 signalling axis in breast cancer cells. Journal of Cellular and Molecular Medicine, 21(4), 720-734.

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Protein Analysis of CD4+ T Cells

Cited 1 time

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For protein analysis of tissues, tissue was suspended in a Triton lysis buffer, homogenized and ELISA was performed. CD4⁺ T cells were lysed and protein detected by western blot as per Hedl et al. (2016) (link) with antibodies to: IRF5 (Abcam, for mouse) or (E1N9G, Cell signaling Technology, for human), p-IRF5 (ThermoFisher Scientific), p-ERK, ERK, p-ZAP70, ZAP70, p-PLCγ1, PLCγ1, p-Lck, Lck, p-p38, SLP76, and VAV1, all from Cell Signaling, and p38, p-JNK, JNK all from Santa Cruz. IRF5 or VAV1 was immunoprecipitated from CD4⁺ T cells with antibodies to IRF5 (Abcam) or VAV1 (Cell Signaling Technology) bound to protein G or protein A Sepharose (MilliporeSigma). Immunoprecipitates were blotted for the antibodies as above. GAPDH antibodies ([mouse], MilliporeSigma; [rabbit], Cell Signaling Technology), α-tubulin, TATA binding protein [TBP] (Santa Cruz Biotechnology) or the respective protein in whole cell lysate served as loading controls. For intracellular expression by flow cytometry, cells were fixed with Lyse/Fix Buffer (BD Biosciences) for 15 min, permeabilized for 1h with Perm Buffer III (BD Biosciences), washed and then stained with the indicated antibodies. Isotype controls were included for treated cells.

Yan J., Pandey S.P., Barnes B.J., Turner J.R, & Abraham C. (2020). T Cell-Intrinsic IRF5 Regulates T Cell Signaling, Migration, and Differentiation and Promotes Intestinal Inflammation. Cell reports, 31(13), 107820.

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Western Blot Analysis of NF-κB Proteins

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Nuclear and cytoplasmic extracts were fractionated by SDS-PAGE gel as previously described [38] (link). Proteins were transferred and immobilised on nitrocellulose membranes. Membranes were incubated with specific antibodies directed against NF-κB p65, β-actin, TATA-binding protein (All from Santa Cruz Biotechnology), acetylated p65-lysine 310 (Abcam, Cambridge, UK), Brd2 and Brd4 (Bethyl Lab, Montgomery, TX, USA). After washing, membranes were incubated with horseradish peroxidase-linked anti-rabbit immunoglobulin (DAKO Ltd, Ely, UK) and detected by enhanced chemiluminescence (ECL) (GE healthcare, Amersham, UK). The membranes were exposed to X-ray and the bands density was quantified using the GelDoc Imaging System (UVP, Upland, CA). This was standardised against the loading controls and the data were represented in graphs.

Khan Y.M., Kirkham P., Barnes P.J, & Adcock I.M. (2014). Brd4 Is Essential for IL-1β-Induced Inflammation in Human Airway Epithelial Cells. PLoS ONE, 9(4), e95051.

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Immunoblotting Analysis of PRMT-2, DDAH-2, and HIF-1α

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Immunoblotting was done, as mentioned earlier. 4 Total or nuclear lysate was prepared from BEAS2B cells after respective induction, run on 10% SDS-PAGE, and then transferred onto a polyvinylidene difluoride membrane (MDI, Ambala Cantt, India). Blots were incubated with primary mAbs for PRMT-2, DDAH-2, HIF-1a, TFAM and PGC-1a. Anti-rabbit or anti-mouse secondary antibodies (Sigma) conjugated with horseradish peroxidase (HRP) were used, and diaminobenzidine (DAB) along with H 2 O 2 was used as a substrate. TATA-binding protein and a-tubulin were used as loading controls for nuclear and total cell lysate, respectively (both from Santa Cruz Biotechnology, Dallas, Tex). Densitometry was performed with ImageJ software.

Pattnaik B., Bodas M., Bhatraju N.K., Ahmad T., Pant R., Guleria R., Ghosh B, & Agrawal A. (2016). IL-4 promotes asymmetric dimethylarginine accumulation, oxo-nitrative stress, and hypoxic response-induced mitochondrial loss in airway epithelial cells. The Journal of allergy and clinical immunology, 138(1).

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