Mouse monoclonal p53

Manufactured by Santa Cruz Biotechnology

Sourced in United Kingdom, United States

Mouse monoclonal p53 is a laboratory reagent used to detect the presence and localization of the p53 protein in biological samples. p53 is a tumor suppressor protein that plays a crucial role in regulating cell growth and division. This product can be used in various applications, such as Western blotting, immunohistochemistry, and flow cytometry, to study the expression and function of p53 in different cell types and experimental models.

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Lab products found in correlation

Hrp conjugated goat anti mouse igg, by Santa Cruz Biotechnology (2 mentions) Lsm 510, by Zeiss (1 mentions) Hoechst 33258, by Thermo Fisher Scientific (1 mentions) Yoyo 1, by Thermo Fisher Scientific (1 mentions) Axio imager m1, by Zeiss (1 mentions) Hmgb1, by Abcam (1 mentions) Lsm 880, by Leica (1 mentions) Goat anti mouse cy3, by Jackson ImmunoResearch (1 mentions) Image studio 2, by LI COR (1 mentions) Protein assay dye reagent, by Bio-Rad (1 mentions) Rabbit polyclonal cleaved caspase 3, by Cell Signaling Technology (1 mentions) Complete protease inhibitor cocktail, by Roche (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Mouse monoclonal pcna, by Cell Signaling Technology (1 mentions) Chemidoc xrs imaging system, by Bio-Rad (1 mentions) Goat anti rabbit igg, by Santa Cruz Biotechnology (1 mentions) Goat anti mouse igg, by Santa Cruz Biotechnology (1 mentions) Restore western blot stripping buffer, by Thermo Fisher Scientific (1 mentions) Supersignal west pico chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) 5 5 6 6 tetrachloro 1 1 3 3 tetraethylbenzimidazolylcarbocyanine iodide jc 1, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Mouse monoclonal anti-p53 (19 citations) Mouse monoclonal anti-p53 (DO-1) (15 citations) Mouse monoclonal anti-p53 antibody (9 citations) Anti-p53 (B-P3; mouse monoclonal; sc-65334 (2 citations) P53 mouse monoclonal antibody (2 citations) Mouse monoclonal anti-human p53 (2 citations) Mouse monoclonal anti-p53 (clone DO-1, (2 citations) Mouse monoclonal anti-p53 DO-1 antibody (2 citations) Mouse monoclonal anti-p53 [sc-126], (2 citations)

6 protocols using mouse monoclonal p53

Immunohistochemical Analysis of Neuronal Markers

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Twenty µm-thick coronal sections were cut on a freezing cryostat. Sections obtained were cryoprotected in 30% sucrose solution for two days. Sections were then immunolabeled with mouse monoclonal NeuN (1:200, Chemicon), rabbit polyclonal HMGB1 (1:200, Abcam), mouse monoclonal p53 (1:100, Santa Cruz) and rabbit polyclonal phospho-serine15-p53 antibody (1:100, Abcam), followed by secondary labeling with goat anti-mouse Cy3 (1:200, Jackson Immunoresearch) or goat anti-rabbit Cy2 antibody (1:200, Jackson Immunoresearch). In order to increase signal from poorly fixed sections, we used EDTA antigen retrieval (1 mM) at 95 °C for 10 minutes and added 0.3 M glycin to blocking solution to decrease non-specific staining. Sections were mounted with medium containing 1 µL/mL of Hoechst-33258 or YOYO-1 or TO-PRO-3 (Thermo Fisher Scientific). Sections were examined under a fluorescent microscope (Nikon E600) at different magnifications with appropriate filter settings. Representative sections were also imaged under laser scanning confocal microscope (Carl Zeiss LSM 510 and LSM 880 system equipped with fast airy scan detector, or Leica SP8) and with differential interference microscopy (DIC) (Carl Zeiss Axioimager M1).

Dehghani A., Karatas H., Can A., Erdemli E., Yemisci M., Eren-Kocak E, & Dalkara T. (2018). Nuclear expansion and pore opening are instant signs of neuronal hypoxia and can identify poorly fixed brains. Scientific Reports, 8, 14770.

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Western Blot Analysis of Apoptosis Markers

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Cell lysates were prepared in radioim-munoprecipitation assay buffer [20 mmol/l Tris-HCl (pH 7.5), 0.1% (w/v) sodium lauryl sulfate, 0.5% (w/v) sodium deoxycholate, 135 mmol/l NaCl, 1% (v/v) Triton X-100, 10% (v/v) glycerol, 2 mmol/l EDTA] supplemented with Complete protease inhibitor cocktail (Roche Molecular Biochemicals) and phosphatase inhibitors sodium fluoride (20 mmol/l) and sodium vanadate (0.27 mmol/l). Western blot analysis was performed as previously described (20 (link)). The total protein concentration was determined using the protein assay dye reagent from Bio-Rad Laboratories. Cell lysates in SDS-sample buffer were boiled for 5 min and equal amounts of total protein were analyzed by 10% SDS-PAGE and western blotting. The antibodies used in this study are mouse monoclonal p53 (1:250) from Santa Cruz Biotechnology; rabbit polyclonal cleaved caspase-3 (1:1,000), rabbit polyclonal cleaved PARP (1:1,000), mouse monoclonal GAPDH (1:1,000), and mouse monoclonal PCNA (1:1000) from Cell Signaling Technology. Proteins were detected using the Odyssey Infrared Imaging System (LI-COR Biosciences, Lincoln, NB, USA) and analyzed with Licor Image Studio 2.0 acquisition and analysis software.

LANGE I., MOSCHNY J., TAMANYAN K., KHUTSISHVILI M., ATHA D., BORRIS R.P, & KOOMOA D.L. (2016). Scrophularia orientalis extract induces calcium signaling and apoptosis in neuroblastoma cells. International Journal of Oncology, 48(4), 1608-1616.

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Western Blot Analysis of Protein Expression

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Forty micrograms of total protein from each rat was separated on 10.5% SDS-polyacrylamide gels by electrophoresis and transferred to PVDF membranes in a BioRad mini tank apparatus (Ou et al., 2011 (link)). After transfer, the membranes were blocked at room temperature for 1h with 5% nonfat dry milk. Membranes were then incubated with either rabbit polyclonal anti-PKR (Santa Cruz, Dallas, TX), rabbit monoclonal anti-p-PKR (Abcam, Cambridge, UK), rabbit monoclonal IFNγ (Abcam), or mouse monoclonal p53 (Santa Cruz) primary antibodies overnight at 4 °C. Following incubation with respective HRP-conjugated secondary antibodies, goat anti-mouse IgG or goat anti-rabbit IgG (Santa Cruz), bands were visualized by horseradish peroxidase reaction using SuperSignal West Pico Chemiluminescent Substrate (Thermo Scientific). Following band visualization, the membrane was stripped for 20 min at room temperature in Restore Western Blot Stripping Buffer (Thermo Scientific), blocked, washed, then re-probed with mouse anti-actin primary antibody (1:10,000; Millipore) and HRP-conjugated goat anti-mouse IgG (Santa Cruz) as a control for sample loading. Protein bands were visualized by the ChemiDoc XRS+ Imaging System (BioRad). The optical density of the autoradiographic bands was calculated and normalized to those of actin using Quantity One Plus analysis software (Ou et al., 2011 (link)).

Duncan J.W., Johnson S., Zhang X., Zheng B., Luo J., Ou X.M., Stockmeier C.A, & Wang J.M. (2016). Upregulation of PKR signaling pathway by ethanol displays an age of onset dependent relationship. Alcoholism, clinical and experimental research, 40(11), 2320-2328.

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Comprehensive Molecular Profiling of Cell Death

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3-Bromopyruvate (3BP), ATP Bioluminescent Assay Kit, 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide (MTT), 2′,7′-dichlorodihydrofluorescein diacetate (H₂DCFDA), MitoTEMPO, antimycin A, menadione, perifosine, digitonin, staurosporine, erythrosin B, LC3 rabbit polyclonal antibody, and actin mouse monoclonal antibody were from Sigma Aldrich. Cyt c mouse monoclonal, COX-IV mouse monoclonal, p53 mouse monoclonal, goat anti-mouse HRP-conjugated IgG, goat anti-rabbit HRP-conjugated IgG, and rabbit anti-goat HRP-conjugated IgG antibodies were from Santa Cruz Biotechnology. Akt rabbit polyclonal, p-Akt (Ser-473) rabbit monoclonal, JNK rabbit monoclonal, p-JNK (Thr183/Tyr185) rabbit monoclonal, p44/42 MAPK (ERK1/2) rabbit monoclonal, p-ERK1/2 (Thr202/Tyr204) rabbit monoclonal, p38 MAPK rabbit polyclonal, p-p38 (Thr180/Tyr182) rabbit monoclonal, p-p53 (Ser-15) rabbit polyclonal, caspase-3 rabbit polyclonal, and caspase-9 rabbit polyclonal antibodies were from Cell Signaling Technology. Beta tubulin mouse monoclonal antibody was from Proteintech. 5,5′,6,6′-tetrachloro-1,1′,3,3′tetraethylbenzimidazolylcarbocyanine iodide (JC-1) and MitoSOX™ were from Molecular Probes.

Petricciuolo M., Davidescu M., Fettucciari K., Gatticchi L., Brancorsini S., Roberti R., Corazzi L, & Macchioni L. (2020). The efficacy of the anticancer 3-bromopyruvate is potentiated by antimycin and menadione by unbalancing mitochondrial ROS production and disposal in U118 glioblastoma cells. Heliyon, 6(12), e05741.

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Molecular Mechanisms Modulating Cancer Cell Responses

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The drugs were dissolved in DMSO at the final concentration of 10 mM. Imatinib was purchased from Cayman Chemical (Michigan, USA) and used in the range of 5–25 µM; Gemcitabine was obtained from Sigma Aldrich Corp. (St Louis, MO, USA) and used in the range of 1–10 µM; Cisplatin, kindly donated by Prof. Justin Stebbing (Imperial College, London), was used in the range 1–25 µM. The following antibodies were used: MSLN mouse monoclonal (Santa Cruz); β-actin mouse monoclonal (Abcam), p53 mouse monoclonal (Santa Cruz); pERK, mouse polyclonal (Abcam); PARP rabbit polyclonal (Cell Signaling); pAKT rabbit polyclonal (Abcam); ERK1-2 rabbit polyclonal (Abcam); Secondary HRP (horseradish peroxidase)-conjugated goat anti-rabbit IgG and goat antimouse IgG antibodies were from GE Healthcare. The expression plasmid pcDNA3.1 encoding for MSLN (aa 360-2230) was kindly donated by Dr. Uehara (Kansai Medical University, Japan); the empty vector pcDNA3.1, employed as control, was donated by Dr. Giamas (Imperial College, London).

Melaiu O., Stebbing J., Lombardo Y., Bracci E., Uehara N., Bonotti A., Cristaudo A., Foddis R., Mutti L., Barale R., Gemignani F., Giamas G, & Landi S. (2014). MSLN Gene Silencing Has an Anti-Malignant Effect on Cell Lines Overexpressing Mesothelin Deriving from Malignant Pleural Mesothelioma. PLoS ONE, 9(1), e85935.

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TNBC Cell Lines and Irradiation Protocol

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TNBC model cells (MDA-MB-231 and MDA-MB-468) were purchased from the American-Type Culture Collection (ATCC) and maintained in RPMI 1640 and DMEM medium supplemented with 10% fetal bovine serum, respectively (Sigma-Aldrich, St. Louis, MO). HEK-293T cells were obtained from ATCC and maintained in DMEM supplemented with 10% fetal bovine serum. MDA-MB-231 cells expressing control- or PELP1-shRNA were generated as described earlier (22 (link)). Non-targeted and SMARTpool PELP1siRNA were obtained from Dharmacon Inc. (Lafayette, CO). The p53 (mouse monoclonal) and E2F1 mouse monoclonal antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA). The PELP1 antibody was purchased from Bethyl laboratories (Montgomery, TX). Cleaved Caspase-3, cleaved PARP-1, and p53 antibody was purchased from Cell Signaling Technologies (Beverly, MA). The phospho-PELP1 antibody was generated as described previously (24 (link)). GFP-TRAP beads were obtained from ChromoTek (Planegg-Martinsried, Germany). Cisplatin (cis-Diamineplatinum (II) dichloride), carboplatin, and camptothecin were purchased from Sigma-Aldrich (St. Louis, MO, USA). For the radiation treatment, the exponentially growing cells were exposed to various doses of ¹³⁷Cs -rays at a dose rate of 0.93 Gy/min at room temperature using a Gamma Cell-40 irradiator (Atomic Energy of Canada Ltd, Montreal, Canada).

Krishnan S.R., Nair B.C., Sareddy G.R., Roy S.S., Natarajan M., Suzuki T., Peng Y., Raj G, & Vadlamudi R.K. (2015). Novel role of PELP1 in regulating chemotherapy response in mutant p53-expressing triple negative breast cancer cells. Breast cancer research and treatment, 150(3), 487-499.

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