Anti ctbp1

Manufactured by BD

Sourced in United States

Anti-CtBP1 is a laboratory product that can be used to detect and quantify the CtBP1 protein. CtBP1 is a transcriptional co-repressor involved in various cellular processes. The anti-CtBP1 product can be used in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry to study the expression and localization of CtBP1 in biological samples.

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Lab products found in correlation

Anti ctbp2, by BD (5 mentions) Ripa buffer, by Merck Group (2 mentions) Anti flag, by Merck Group (2 mentions) Anti p300, by Santa Cruz Biotechnology (2 mentions) Anti myc, by Abcam (2 mentions) Anti gapdh, by Thermo Fisher Scientific (2 mentions) Anti cyclin d1, by Santa Cruz Biotechnology (1 mentions) Pierce ecl western blotting substrate, by Thermo Fisher Scientific (1 mentions) Anti cd68, by Thermo Fisher Scientific (1 mentions) Anti cd31, by Thermo Fisher Scientific (1 mentions) Anti gapdh, by Santa Cruz Biotechnology (1 mentions) Anti dnmt3a, by Abcam (1 mentions) Anti dnmt1, by Abcam (1 mentions) Anti caspase 1, by Santa Cruz Biotechnology (1 mentions) Anti p65, by Thermo Fisher Scientific (1 mentions) Anti c fos, by Merck Group (1 mentions) Anti nlrp3, by Abcam (1 mentions) Anti il 1β, by Abcam (1 mentions) Anti irf2, by Abcam (1 mentions) Anti stat4, by Abcam (1 mentions)

Spelling variants of this product

CTBP1 (4 citations) Mouse anti-CtBP1 (2 citations) Anti-CtBP1 antibody (2 citations)

7 protocols using anti ctbp1

High-fat Diet Impacts Xenograft Tumor Growth

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All animal experiments followed the institutional guidelines for animal welfare. Four-week-old athymic male Swiss nu/nu mice were fed for 16 weeks with control diet (CD) (n = 18) or HFD (n = 18). Chow food was supplemented with bovine fat in a 2:1 proportion (w/w) to generate HFD. CD and HFD had 3 or 5 kcal per gram of food, respectively. After 12 weeks of diet, each CD- and HFD-fed mice group were randomly divided and subcutaneously injected with PC3.pGIPZ or PC3.shCtBP1 cells (4.8 × 10⁶). Body weight was determined three times a week. Tumor size was measured for 4 to 6 weeks and tumor volume was calculated as described (19 (link)). At necropsy, blood was drawn from all mice by direct heart puncture; serum was separated and tumors were excised. Tissues were formalin fixed and paraffin embedded. Histopathology and IHC studies were performed in 5 μm tissue sections using hematoxylin and eosin (H&E) or specific antibodies: anti-CtBP1 (BD Biosciences); anti-BRCA1 (ARP33338_P050, Aviva System Biology), anti-E-cadherin (Clone HECD-1, Zymed Laboratories Inc); and anti-cyclin D1 (H295, Santa Cruz Biotechnologies).
Serum cholesterol, triglycerides, glycemia, NAD⁺/NADH levels, testosterone, and estradiol determinations were performed as described in Supplementary Methods.

Moiola C.P., De Luca P., Zalazar F., Cotignola J., Rodríguez-Seguí S.A., Gardner K., Meiss R., Vallecorsa P., Pignataro O., Mazza O., Vazquez E.S, & De Siervi A. (2014). Prostate Tumor Growth Is Impaired by CtBP1 Depletion in High-Fat Diet–Fed Mice. Clinical cancer research : an official journal of the American Association for Cancer Research, 20(15), 4086-4095.

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Immunoblot Analysis of Cell and Tissue Proteins

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The immunoblot analysis was performed as described previously 35 (link). Briefly, tissues and cells were lysed in 1×RIPA buffer (Sigma-Aldrich, #R0278). Equal amounts of protein in each sample were loaded into a 10% SDS-PAGE gel. After transferring to a membrane and blocking with 5% milk, the proteins were probed with the following primary antibodies: anti-CtBP1 (BD Biosciences, San Jose, CA, USA, #612042), anti-CtBP2 (BD Biosciences, #612044), anti-CD31 (ThermoFisher Scientific, #PA5-16301), anti-CD55 (ThermoFisher Scientific, #PA5-82005), anti-CD68 (ThermoFisher Scientific, #MA5-13324), anti-GAPDH (Santa Cruz Biotechnology, Dallas, Texas, USA, #sc-365062), anti-Caspase-1 (Santa Cruz Biotechnology, #sc-56036), anti-Flag (Sigma-Aldrich, #SAB4200071), anti-Myc (Abcam, Cambridge, MA, USA, #ab9106), anti-p300 (Santa Cruz Biotechnology, #sc-585), anti-c-Jun (Sigma-Aldrich, #SAB4501606), anti-c-FOS (Sigma-Aldrich, #F7799), anti-p50 (ThermoFisher Scientific, #PA1-30409), anti-p65 (ThermoFisher Scientific, #14-6731-81), anti-IRF2 (Abcam, #ab3388), anti-STAT4 (Abcam, #ab68156), anti-NLRP3 (Abcam, #ab210491), anti-Il-1β (Abcam, #ab2105), anti-DNMT1 (Abcam, #ab13537), and anti-DNMT3A (Abcam, #ab2850). After probing with secondary antibodies, protein band signals were detected using a Pierce^TM ECL western blotting substrate (ThermoFisher Scientific, #32106).

Sun X., Xiao L., Chen J., Chen X., Chen X., Yao S., Li H., Zhao G, & Ma J. (2020). DNA methylation is involved in the pathogenesis of osteoarthritis by regulating CtBP expression and CtBP-mediated signaling. International Journal of Biological Sciences, 16(6), 994-1009.

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ChIP Assay for Chromatin Precipitation

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The ChIP assay was performed as previously described 45 . Briefly, cells were washed once with 1x PBS at room temperature and then crosslinked with 1x PBS containing 1% formaldehyde for 30 minutes. The fixed cells were sonicated to an average size of 300-500 bp, and cell lysates were subjected to chromatin precipitation with a Millipore ChIP Assay Kit (Millipore, USA, #17295) following the manufacturer's protocol. Chromatin fragments were immunoprecipitated with the following antibodies: anti-CtBP1 (#612042) and anti-CtBP2 (#612044) from BD Biosciences, mouse IgG (#sc-2025), anti-Pol II (#sc-47701), anti-HDAC1 (#sc-8410), anti-acetyl-histone H3 (#sc-8655), anti-p300 (#sc-585) and anti-Runx2 (#sc-101145) from Santa Cruz Biotechnology. The immunoprecipitated DNA was analyzed by qRT-PCR using the primers listed in Supplementary Table 3.

Zhang W., Duan N., Zhang Q., Song T., Li Z., Chen X, & Wang K. (2018). The intracellular NADH level regulates atrophic nonunion pathogenesis through the CtBP2-p300-Runx2 transcriptional complex. International Journal of Biological Sciences, 14(14), 2023-2036.

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Proteomic Analysis of Pancreatic Biopsies

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Three-paired pancreatic biopsies from pancreatic cancer patients (stage 0) and AP patients and cultured cells were used for protein extraction with 1 × RIPA buffer (Sigma-Aldrich, St. Louis, MO, USA, #R0278). Total protein concentrations were determined using a Nanodrop spectrophotometer (Thermo Fisher Scientific, #ND-2000) at 280 nm. Equal amounts of total proteins were loaded onto 12% SDS-PAGE gels for electrophoretic separation. Proteins were then transferred to polyvinylidene difluoride (PVDF) membranes (GE Healthcare, Chicago, IL, USA, #10600023), followed by blocking with 5% milk for 1 h and then probing with primary antibodies including anti-c-MYC (Sigma-Aldrich, #06-340), anti-PCAF (Sigma-Aldrich, #SAB2101734), anti-CtBP1 (BD Biosciences, San Jose, CA, USA, #612042), anti-CtBP2 (BD Biosciences, #612044), anti-Myc (Abcam, Shanghai, China, #ab206486), anti-Flag (Sigma-Aldrich, #SAB4200071), anti-DNMT1 (Sigma-Aldrich, #D4692), anti-DNMT3a (Sigma-Aldrich, #SAB1410305), anti-DNMT3b (Sigma-Aldrich, #SAB2700189), and anti-GAPDH (Abcam, #ab8254). After washing with TBST buffer 5 times, the membrane was further probed with secondary antibodies. Protein signals were recorded with a ChemiDoc Imaging System from Bio-Rad (Hercules, CA, USA).

Zeng J., Chen J.Y., Meng J, & Chen Z. (2020). Inflammation and DNA methylation coregulate the CtBP-PCAF-c-MYC transcriptional complex to activate the expression of a long non-coding RNA CASC2 in acute pancreatitis. International Journal of Biological Sciences, 16(12), 2116-2130.

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Comprehensive Western Blotting Analysis

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Western blotting analysis was performed following a previously described method 20 (link). Briefly, cells were lysed in radioimmunoprecipitation assay (RIPA) buffer (Sigma-Aldrich, #R0278) containing protease inhibitor (Sigma-Aldrich, P8340). Equal amounts of total proteins were loaded and resolved by SDS-PAGE gels, followed by transferring to a PVDF membrane, blocking with 5% milk, and probing with primary antibodies. The following primary antibodies were used: anti-CtBP1 (BD Bioscience, USA, #612042), anti-CtBP1 (phospho Ser422) (GeneTex, USA, #GTX55356), anti-CtBP2 (BD Bioscience, #612044), anti-HIPK2 (Cell Signaling, USA, #5091S), anti-BIM (Abcam, China, #ab170589), anti-BIK (Abcam, #ab52182), anti-BAX (Abcam, #ab3191), anti-NOXA (Abcam, #114C307), anti-CASP3 (Sigma-Aldrich, #C9598), anti-CASP7 (Sigma-Aldrich, #C1104), anti-CASP9 (Abcam, #ab184786), anti-p300 (Sigma-Aldrich, #P2859), anti-FOXO3a (Sigma-Aldrich, #V38041), and anti-GAPDH (Thermo Fisher Scientific, #MA5-15738-BTIN). The protein signals were visualized using an ECL detection kit (Sigma-Aldrich, #GERPN2109).

Duan N., Zhang W., Li Z., Sun L., Song T., Yu Z., Chen X, & Ma W. (2021). Overexpression of HIPK2 removes the transrepression of proapoptotic genes mediated by the CtBP1-p300-FOXO3a complex and increases the chemosensitivity in osteosarcoma cells. Journal of Cancer, 12(6), 1826-1837.

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Western Blot Analysis of Stemness and Drug Resistance

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Cells were washed twice with PBS and lysed with 1 × RIPA buffer (Sigma-Aldrich, #R0278) containing a protease inhibitor cocktail (Sigma-Aldrich, P8340). Equal amounts of total protein (approximately 50 μg) were resolved in 10% SDS-PAGE gels and transferred to PVDF membranes, followed by blocking with 5% skim milk powder dissolved in phosphate buffered saline-Tween20 (PBST) for 1 h at room temperature. Membranes were probed with the following primary antibodies: anti-CD133 (Sigma-Aldrich, #MAB4399-I), anti-CtBP1 (BD Bioscience, San Jose, CA, USA, #612042), anti-FOXM1 (Sigma-Aldrich, #AV39518), anti-MDR1 (Thermo Fisher Scientific, #PA5-28801), and anti-GAPDH (Thermo Fisher Scientific, #MA5-15738-BTIN). After incubating with primary antibodies at 4°C overnight, membranes were washed five times with PBST buffer and then probed with peroxidase-conjugated secondary antibodies (Abcam, Cambridge, UK; mouse, #ab205719; and rabbit, #ab205718) for 1 h at room temperature. The protein signals were visualized using an ECL detection reagent (Sigma-Aldrich, #GERPN2109).

Chen X., Zhang Q., Dang X., Song T., Wang Y., Yu Z., Zhang S., Fan J., Cong F., Zhang W, & Duan N. (2021). Targeting the CtBP1-FOXM1 transcriptional complex with small molecules to overcome MDR1-mediated chemoresistance in osteosarcoma cancer stem cells. Journal of Cancer, 12(2), 482-497.

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Protein Extraction and Western Blot Analysis

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Total protein extracts were prepared as previously described (Fedele et al., 2017 (link)). For lysates preparation from frozen GBM samples, small pieces in the range of 0.02 to 0.05 grams were selected, washed with cold PBS Buffer and then treated with RIPA buffer, containing Phosphatase/Protease Inhibitors and PMSF. The tissues were disrupted using pestles and then processed according to our standard protocol (Fedele et al., 2017 (link)). Cytoplasmic and nuclear extracts were prepared using a Nuclear Extract Kit (Active Motif) according to the manufacturer’s instructions. Western blots were performed using the following antibodies: anti-ZBTB18 (Abcam # ab118471); anti-ZNF238 (Sigma # SAB1406998); anti-FLAG M2 (Sigma #F1804); anti-FLAG (Cell Signaling Technologies #14793), anti-HA (Abcam ##18181), anti-CTBP1 (BD Biosciences #612042); anti-CTBP2 (BD Biosciences #612044); anti-CAPN2 (Cell Signaling Technologies #2539S); anti-CAST (Cell Signaling #4146S) anti-alpha Tubulin (Abcam #ab7291) and anti-Laminin B (Santa Cruz #sc-6216), anti Lamin A/C (Cell Signaling Technologies ##4777). The quantification of western blot bands was performed using the ImageJ software (Biorad) and normalized to the level of αTubulin.

Masilamani A.P., Schulzki R., Yuan S., Haase I.V., Kling E., Dewes F., Andrieux G., Börries M., Schnell O., Heiland D.H., Schilling O., Ferrarese R, & Carro M.S. (2022). Calpain-mediated cleavage generates a ZBTB18 N-terminal product that regulates HIF1A signaling and glioblastoma metabolism. iScience, 25(7), 104625.

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