Anti tbp

Manufactured by Cell Signaling Technology

Sourced in United States

Anti-TBP is a laboratory reagent used to detect and quantify the TATA-binding protein (TBP) in biological samples. TBP is a key component of the transcription initiation complex and plays a crucial role in regulating gene expression. The Anti-TBP product is a highly specific antibody designed to specifically bind and detect TBP, enabling researchers to study its expression and localization in various experimental systems.

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Lab products found in correlation

Anti gapdh, by Cell Signaling Technology (4 mentions) Anti akt, by Cell Signaling Technology (2 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Immunoprecipitation kit, by Merck Group (1 mentions) Pierce magnetic rna protein pull down kit, by Thermo Fisher Scientific (1 mentions) Ribo rnamax t7 biotin labeled transcription kit, by RiboBio (1 mentions) Q exactive mass spectrometer, by Thermo Fisher Scientific (1 mentions) Anti p iκbα, by Cell Signaling Technology (1 mentions) Anti pcdk9, by Cell Signaling Technology (1 mentions) Anti cyclin t1, by Cell Signaling Technology (1 mentions) Anti cdk9, by Cell Signaling Technology (1 mentions) Ecl chemiluminescence system, by Santa Cruz Biotechnology (1 mentions) Anti p65, by Santa Cruz Biotechnology (1 mentions) Anti α tubulin, by Cell Signaling Technology (1 mentions) Anti iκbα, by Cell Signaling Technology (1 mentions) Anti vegf, by Abcam (1 mentions) Ripa buffer, by Merck Group (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Anti β actin, by Merck Group (1 mentions) Protease inhibitor, by Merck Group (1 mentions)

8 protocols using anti tbp

RNA-Protein Interaction Profiling

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Biotinylated RNAs were harvested by using a Ribo RNAmax-T7 biotin-labeled transcription kit (RiboBio, China). A Pierce Magnetic RNA–Protein Pull-Down Kit (Thermo Fisher Scientific) was used in RNA–protein pull-down experiments according to the manufacturer’s instructions. The eluted products were identified by mass spectrometry with a Q Exactive mass spectrometer (Thermo Fisher) or western blot.
Immunoprecipitation Kit (Millipore, USA) according to the manufacturer’s instructions. The antibody used for RIP assays was anti-TBP (44059, Cell Signaling, 1:100).

Ma M., Cai B., Zhou Z., Kong S., Zhang J., Xu H., Zhang X, & Nie Q. (2023). LncRNA-TBP mediates TATA-binding protein recruitment to regulate myogenesis and induce slow-twitch myofibers. Cell Communication and Signaling : CCS, 21, 7.

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Immunoblot Analysis of NF-κB Pathway

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C11 cells were adjusted to 1 × 10⁶ cells/ml and stimulated with 1 μM prostratin or 0.05 μM EK-16A for various time. Whole-cell extracts or the nuclear fractions were prepared as described previously^{99 (link), 100 (link)}. Proteins were separated by SDS-PAGE, transferred to nitrocellulose membrane, and visualized with primary and secondary antibodies and ECL chemiluminescence system (Santa Cruz Biotechnology, Santa Cruz, CA). The following primary antibodies were used: anti-IκBα (catalog # 9242), anti-p-IκBα (# 9246), anti-CDK9 (# 2316), anti-p-CDK9 (# 2549), anti-Cyclin T1 (# 8744), anti-α-Tubulin (# 2125), anti-TBP (# 12578) (Cell Signaling, Danvers, MA), and anti-p65 (catalog # sc-56735; Santa Cruz).

Wang P., Lu P., Qu X., Shen Y., Zeng H., Zhu X., Zhu Y., Li X., Wu H., Xu J., Lu H., Ma Z, & Zhu H. (2017). Reactivation of HIV-1 from Latency by an Ingenol Derivative from Euphorbia Kansui. Scientific Reports, 7, 9451.

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Western Blot Analysis of Tumor Samples

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For in vitro samples, cells were prepared and Western blot was performed as described previously [29] (link). In vivo tumor samples were first crushed using a homogenizer in a protein cocktail containing RIPA buffer (Millipore, Billerica, MA), protease inhibitors, and phosphatase inhibitors (Sigma-Aldrich, St Louis, MO). Then, the samples were centrifuged for 15 minutes at 14,000 rpm and 4°C. The following preparation steps follow the same protocol as the in vitro samples [29] (link). Blots were probed with anti-CD31, anti-VEGF (Abcam, Cambridge, MA), anti-c-MYC, or anti–hypoxia inducible factor 1-alpha /(HIF-1α) (Abcam) and their appropriate secondary antibodies. Blots were then probed with anti–β-actin (Sigma-Aldrich) or anti-TBP (Cell Signaling Technology, Boston, MA), and the β-actin or TBP to protein ratios were calculated to allow for standardized comparisons.

Lee J.G, & Wu R. (2015). Erlotinib-Cisplatin Combination Inhibits Growth and Angiogenesis through c-MYC and HIF-1α in EGFR-Mutated Lung Cancer In Vitro and In Vivo. Neoplasia (New York, N.Y.), 17(2), 190-200.

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Western Blotting Analysis of Notch Signaling

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Fractionated cell lysates were prepared using a NE-PER Nuclear and Cytoplasmic Extraction kit (Thermo Scientific) and subjected to Western blotting using anti-NOTCH1 (anti-TAD; [16 (link)]), anti-V1744 antibody recognizing S3-cleaved NOTCH1 (Cell Signaling #4147); anti-Notch3 (Cell Signaling #2889); a polyclonal anti-Notch3 antibody raised against the neoepitope generated by S3 cleavage of NOTCH3; anti-TBP (Cell Signaling #8515); or anti-GAPDH (Cell Signaling #2118). The polyclonal anti-Notch3 antibody recognizing S3-cleaved NOTCH3 was raised against the KLH conjugated peptide epitope (VMVARRKREHSTLWFPG) (Covance) and affinity purified using a peptide epitope-coupled resin.

Choi S.H., Severson E., Pear W.S., Liu X.S., Aster J.C, & Blacklow S.C. (2017). The common oncogenomic program of NOTCH1 and NOTCH3 signaling in T-cell acute lymphoblastic leukemia. PLoS ONE, 12(10), e0185762.

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Molecular Mechanisms of Glioblastoma Therapy

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PP was provided by MedChem Express (Princeton, NJ, USA). CHIR-99021 was provided by Selleckchem Company (Houston, TX, USA). TMZ and lithium chloride were provided by Sigma (St. Louis, MO, USA). The anti-Cleaved Caspase-3, anti-Caspase 9, anti-Bcl-2, anti-Bax, anti-Survivin, anti-cyclin B1, anti-cyclin D1, anti-β-catenin, anti-p-β-catenin (S552), anti-p-β-catenin (S33/37/T41), anti-GSK-3β, anti-p-GSK-3β (Ser9), anti-AKT, anti-p-AKT, anti-TBP, anti-GAPDH, and anti-histone H3 antibodies were provided by Cell Signaling Technology (Beverly, MA, USA). The anti-MGMT and anti-β-actin antibodies were provided by Abcam (Cambridge, MA, USA). The anti-p-GSK3β (Y216) antibody was provided by Thermo (Invitrogen, CA, USA). The anti-PARP-1 antibody was provided by Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Li H., Liu S., Jin R., Xu H., Li Y., Chen Y, & Zhao G. (2021). Pyrvinium pamoate regulates MGMT expression through suppressing the Wnt/β-catenin signaling pathway to enhance the glioblastoma sensitivity to temozolomide. Cell Death Discovery, 7, 288.

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Histone and Nuclear Protein Extraction and Analysis

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Histone extracts were isolated from harvested cells using the EpiQuick Total Histone Extraction Kit (Epigentek) according to the manufacturer’s instructions. Nuclear extracts were isolated from harvested cells using standard nuclear fractionation protocol (Abcam). Protein concentrations were determined by the Lowry protein assay and 2 μg of histone or nuclear extract was used per well. Samples were run on 4–12% Bis-Tris gels (NuPAGE, Thermo-Fisher) in MES-SDS running buffer (NuPAGE, Thermo-Fisher). After 90 min of transfer at 30mV, nitrocellulose membranes were stained overnight at 4°C with anti-H3K27me3 (Cell Signaling, #9733; dilution 1/250), anti-H3 (Active Motif, #61475; dilution 1/5000), anti-Ezh2 (Cell Signaling, #5246; dilution 1/500) and anti-TBP (Cell Signaling, #44059; dilution 1/5000) diluted in blocking buffer (TBS, 0.1% Tween, 5% BSA). Protein detection was performed using HRP-coupled antibodies (Cell Signaling) and the ECL Prime detection reagent (GE Healthcare). Membranes were imaged and quantified using the G:BOX Chemi XT4 and associated software (Syngene).

Dal-Pra S., Hodgkinson C.P., Mirotsou M., Kirste I, & Dzau V.J. (2017). Demethylation of H3K27 Is Essential for the Induction of Direct Cardiac Reprogramming by miR Combo. Circulation research, 120(9), 1403-1413.

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Western Blot Analysis of Signaling Proteins

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Cell lysates were prepared in standard NP-40 lysis buffer (Abcam, USA) supplemented with proteinase and phosphatase inhibitors. Protein lysates were then quantified using the Pierce BCA protein assay kit (Thermo Fisher Scientific, USA). Equal masses of total protein were separated on 4–12% SDS-polyacrylamide mini-gels and blotted onto PVDF membrane (Millipore, USA). Membranes were subsequently blocked, incubated with primary antibodies, and incubated with secondary antibodies according to WesternBreeze Chromogenic Kit (Thermo Scientific, USA). Alkaline phosphatase was detected on the PVDF membranes using a ready-to-use BCIP/NBT substrate (Thermo Scientific, USA) for ready visualization of enzyme-linked antibodies. Rabbit anti-p65, anti-phospho-p65, anti-GAPDH, and anti-TBP antibodies were obtained from Cell Signaling (USA) or Abcam (USA).

Zgheib C., Hodges M.M., Hu J., Liechty K.W, & Xu J. (2017). Long non-coding RNA Lethe regulates hyperglycemia-induced reactive oxygen species production in macrophages. PLoS ONE, 12(5), e0177453.

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Multifaceted Regulation of Cell Metabolism

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BTZ, N-acetylcysteine (NAC), 3-MA and chloroquine (CQ) were purchased from Sigma-Aldrich (St Louis, MO, USA). Tin protoporphyrin IX dichloride (SnPP) was purchased from Santa Cruz Biotechnology (Dallas, TX, USA). Cycloheximide (CHX) was purchased from Beyotime Biotechnology (Shanghai, China). Briefly, BTZ, SnPP and CHX were dissolved in DMSO, respectively; NAC, 3-MA and CQ were dissolved in double distilled water, respectively. For in vivo injection, the BTZ stocks were further diluted in a pyrogen-free sterile 0.9% NaCl solution, and 3-MA was freshly prepared in a pyrogen-free sterile 0.9% NaCl solution.
Anti-human-CD45-FITC was purchased from BD Biosciences (San Jose, CA, USA) for flow cytometry (FCM) analysis. The following antibodies were used for immunoblots: anti-BACH2, anti-AKT, anti-phospho-AKT, anti-HO-1, anti-NRF2, anti-GAPDH, anti-β-Actin and anti-TBP (Cell Signaling, Danvers, MA, USA); anti-LC3 (Novus Biologicals, Littleton, CO, USA) and anti-BACH1 (Santa Cruz Biotechnology, Dallas, TX, USA).

Feng M., Wang J., Sun M., Li G., Li B, & Zhang H. (2021). 3-Methyladenine but not antioxidants to overcome BACH2-mediated bortezomib resistance in mantle cell lymphoma. Cancer Cell International, 21, 279.

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