Anti pcna

Manufactured by Abcam

Sourced in United Kingdom, United States, China

Anti-PCNA is a primary antibody that recognizes the Proliferating Cell Nuclear Antigen (PCNA) protein, a key component involved in DNA replication and repair processes. This antibody can be used as a tool for detecting and quantifying PCNA expression in various cell and tissue samples.

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Lab products found in correlation

Anti ki67, by Abcam (20 mentions) Anti gapdh, by Abcam (16 mentions) Anti cyclin d1, by Abcam (14 mentions) Anti bcl 2, by Abcam (14 mentions) Anti bax, by Abcam (14 mentions) Anti β actin, by Abcam (11 mentions) Anti mmp9, by Abcam (10 mentions) Anti mmp2, by Abcam (9 mentions) Pvdf membrane, by Merck Group (9 mentions) Anti β catenin, by Abcam (6 mentions) Bca protein assay kit, by Thermo Fisher Scientific (6 mentions) Anti cdk2, by Abcam (5 mentions) Anti akt, by Cell Signaling Technology (5 mentions) Anti caspase 3, by Abcam (4 mentions) Anti β actin, by Merck Group (4 mentions) Anti β actin, by Cell Signaling Technology (4 mentions) Anti e cadherin, by Cell Signaling Technology (4 mentions) Anti cleaved caspase 3, by Cell Signaling Technology (4 mentions) Anti p akt, by Cell Signaling Technology (4 mentions) β actin, by Abcam (4 mentions)

Close spelling variants of this product

Anti-PCNA antibody (36 citations) Mouse anti-PCNA (17 citations) Rabbit anti-PCNA (11 citations) Mouse anti-proliferating cell nuclear antigen (PCNA; (5 citations) Rabbit anti-PCNA antibody (4 citations) Mouse anti-human PCNA (2 citations) Anti-PCNA rabbit polyclonal antibody (2 citations) Anti-mouse PCNA antibody (2 citations) Monoclonal anti-PCNA antibody (2 citations) Mouse monoclonal anti-PCNA antibody (2 citations)

142 protocols using anti pcna

Immunofluorescence Analysis of Atrial Tissue

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The atrium tissue samples were fixed and sectioned for analysis as previously described.³¹ The atrium tissue sections were incubated with anti‐PU.1 (1:100; Abcam), anti‐PCNA (5 μg/mL; Abcam) and anti‐α‐SMA (1:50; Cell Signaling Technology) primary antibodies at 4℃ overnight, followed by incubation with a fluorescein isothiocyanate (FITC)–conjugated secondary antibody (1:1000; Cell Signaling Technology) and visualization with an Olympus BX51 microscope (Olympus Corporation).
For immunofluorescence assays of the atrial fibroblasts, the cells were washed with phosphate‐buffered saline (PBS) and fixed with 4% paraformaldehyde for 20 min, followed by permeabilization with 0.1% Triton X‐100 in PBS. The cells were then added to coverslips with a syringe, and the coverslips were blocked with 3% bovine serum albumin for 30 min and then incubated overnight with primary antibodies against PU.1 (1:100; Abcam), anti‐PCNA (5 μg/mL; Abcam) and anti‐α‐SMA (1:50; Cell Signaling Technology). The next day, the coverslips were incubated with a FITC‐conjugated secondary antibody for 1 h, and the nuclei were stained with 4′,6‐diamidino‐2‐phenylindole (DAPI) for 30 min. Cells were then imaged with an Olympus BX51 microscope.

Hu J., Zhang J., Li L., Wang S., Yang H., Fan X., Zhang L., Hu G., Fu H., Song W., Yan L., Liu J., Wu J, & Kong B. (2021). PU.1 inhibition attenuates atrial fibrosis and atrial fibrillation vulnerability induced by angiotensin‐II by reducing TGF‐β1/Smads pathway activation. Journal of Cellular and Molecular Medicine, 25(14), 6746-6759.

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Protein Immunoblotting with Antibodies

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SDS–PAGE-separated proteins were transferred to nitrocellulose membranes and blocked with 5% milk TBS-T (0.05% tween) before incubation with 1:1,000 anti-FANCD2 (Ab2187; Abcam), 1: 5,000 anti-V5 (66007.1-Ig; ProteinTech), or 1: 2,000 anti-PCNA (Ab29; Abcam) overnight at 4°C. Membranes were washed 3× with TBS-T before incubation with secondary antibodies for 1 h at room temperature and washed with TBS-T. Results were visualised on licor using an 800- or 700-nm channel.

Arkinson C., Chaugule V.K., Toth R, & Walden H. (2018). Specificity for deubiquitination of monoubiquitinated FANCD2 is driven by the N-terminus of USP1. Life Science Alliance, 1(5), e201800162.

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Western Blot Analysis of DNA Repair Proteins

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Cells were collected by trypsinization and lysed in RIPA lysis buffer (150 mM NaCl, 1.0% IGEPAL CA-630, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris base, pH 8.0). Phosphatase and protease inhibitors (Gold Biotechnology) were added freshly to the lysis buffer. Following gel electrophoresis and transfer of cell extracts onto nitrocellulose, membranes were incubated for 1 hr or overnight in blocking buffer (5% milk in TBS + 0.1% tween). Membranes were subsequently incubated with primary antibodies diluted in antibody buffer (3% BSA in TBS + 0.1% tween) for 2 hrs at room temperature or overnight at 4°C. Detection was achieved using appropriate horseradish peroxidase (HRP)-conjugated secondary antibodies. Anti-ZRANB3 (1:5,000, Bethyl Laboratories), anti-SMARCAL1 (1:1,000, Santa Cruz Biotechnology), anti-BRCA1 (1:500, Bethyl Laboratories), anti-BRCA2 (1:1,000, Bethyl Laboratories), anti-vinculin (1:100,000, Sigma-Aldrich), anti-β-actin (1:100,000, Novus Biologicals), anti-GAPDH (1:5,000, Novus Biologicals), anti-HLTF (1:2,000, Abcam), anti-LAMIN B1 (Thermo Fisher Scientific), anti-FANCD2 (1:1,000, Novus Biologicals), anti-PCNA (1:100,000, Abcam), anti-NBS1 (GeneTex), anti-MRE11 (Cell Signaling Technology), anti-RPA2 (Bethyl Laboratories) antibodies were used in western blot experiments.

Taglialatela A., Alvarez S., Leuzzi G., Sannino V., Ranjha L., Huang J.W., Madubata C., Anand R., Levy B., Rabadan R., Cejka P., Costanzo V, & Ciccia A. (2017). Restoration of replication fork stability in BRCA1- and BRCA2-deficient cells by inactivation of SNF2-family fork remodelers. Molecular cell, 68(2), 414-430.e8.

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Western Blot Analysis of Apoptosis and Cell Cycle Markers

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Total protein was extracted using RIPA buffer (Beyotime, Shanghai, China) which contained protease and phosphotase inhibitors cocktails. BCA protein assay kit (Beyotime) was used to determine protein concentrations according to the manufacturer’s instructions. Proteins were separated by SDS-PAGE, transferred to PVDF (Millipore, Burlington, MA, USA) membranes, incubated with primary antibodies overnight at 4°C and then incubated with HRP-conjugated secondary antibody (1:5000 dilution) for 1 h in room temperature. Proteins were visualized by using ECL western blotting detection reagents (Millipore). Immunoreactive bands were quantified using ImageJ (NIH, Bethesda, MD, USA).
The primary antibodies used in this study are purchased from Abcam (Cambridge, UK) as followed: anti-Bax (1:1000), anti-Bcl- 2 (1:1000), anti-caspase 3 (1:1000,), anti-caspase 9 (1:1000), anti- Cyclin D1 (1:1000), anti-PCNA (1:1000), anti-Cox-2 (1:1000), anti-MMP2 (1:1000), anti-MMP9 (1:1000), anti-GTPBP4 (1:1000), and anti-β-actin (1:1000, internal control). All reacts with human proteins.

Zhang N., Shen H., Huang S., Wang F., Liu H., Xie F., Jiang L, & Chen X. (2021). LncRNA FGD5-AS1 functions as an oncogene to upregulate GTPBP4 expression by sponging miR-873-5p in hepatocellular carcinoma. European Journal of Histochemistry : EJH, 65(4), 3300.

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Quantification of Apoptosis-Related Proteins

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The concentration of protein was measured by the bicinchoninic acid (BCA) method. Samples with equal amounts of protein were divided via SDS‐PAGE and transferred onto the membranes of PVDF (Millipore). After blocking with 5% skim milk, incubation with primary antibody anti‐Bcl‐2 (1:1000, Abcam), anti‐Bax (1:5000, Abcam), anti‐PCNA (1:5000, Abcam), anti‐14‐3‐3 zeta (namely anti‐YWAHZ, 1:1000, Abcam) and internal control anti‐GAPDH (1:5000, Abcam) at 4°C overnight were performed. The membranes were incubated with secondary antibody (HRP‐conjugated) at room temperature for 1 hour. Immunoreactive bands were visualised using an enhanced chemiluminescence kit (Millipore).

Liu J., Song S., Lin S., Zhang M., Du Y., Zhang D., Xu W, & Wang H. (2019). Circ‐SERPINE2 promotes the development of gastric carcinoma by sponging miR‐375 and modulating YWHAZ. Cell Proliferation, 52(4), e12648.

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Western Blot Analysis of Cellular Proteins

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Total cellular protein (10-20 μg) from each sample was separated by SDS-PAGE, transferred to PVDF membranes and subjected to Western blot analysis. Antibodies for Western blot analysis were obtained by the following commercial sources: anti-ubiquitin (Santa Cruz Biotechnology and Millipore), anti-PCNA (Abcam), anti-PARP (BD Pharmingen), anti-GRP78, anti-GCN2, anti-phospho-eIF2oc, anti-IRE1-α, anti-Ero1L-α, anti-caspase-3 (Cell Signaling), anti-β-actin (Sigma). Peroxidase-linked anti-mouse Immunoglobulin G and peroxidase-linked anti-rabbit Immunoglobulin G were from Amersham.

Coughlin K., Anchoori R., Iizuka Y., Meints J., MacNeill L., Vogel R.I., Orlowski R.Z., Lee M.K., Roden R.B, & Bazzaro M. (2014). Small-Molecule RA-9 Inhibits Proteasome-Associated DUBs and Ovarian Cancer in Vitro and in Vivo Via Exacerbating Unfolded Protein Responses. Clinical cancer research : an official journal of the American Association for Cancer Research, 20(12), 3174-3186.

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Western Blot Analysis of Cellular Proteins

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Total proteins were homogenized with RIPA lysis buffer containing 1 mM phenylmethylsulfonyl fluoride (Solarbio, Beijing, China). After determining the protein concentration, proteins in the supernatant were separated by 10% SDS-PAGE, transferred to polyvinylidene difluoride membranes and then blocked with 5% skim milk for 2 h. After incubating with primary antibodies overnight at 4°C, the membranes were incubated with goat anti-rabbit or anti-mouse horseradish peroxidase-linked secondary antibodies for 2 h. Bands on the membranes were visualized by enhanced chemiluminescence reagents (ECL; Bio-Rad, Hercules, CA, USA). Primary antibodies included anti-PCNA (1:1,000, Abcam, Cambridge, UK), anti-CyclinD1 (1:1,000, Abcam), anti-CDK2 (1:1,000, Abcam), anti-SLC2A1 (1:1,000, Abcam), and anti-β-actin (1:1,000, Abcam), anti-histone H3 (1:1,000, Abcam) and anti-β-tubulin (1:1,000, Abcam).

Li W., Wang S., Shan B., Cheng X., He H., Qin J., Tang Y., Zhao H., Tian M., Zhang X, & Jin G. (2021). CircHECTD1 Regulates Cell Proliferation and Migration by the miR-320-5p/SLC2A1 Axis in Glioblastoma Multiform. Frontiers in Oncology, 11, 666391.

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Quantifying Renal Tissue Immunomarkers

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Histological sections of renal tissue were incubated for 1 h at room temperature with the following antibodies: anti-macrophage cell-surface protein 2 (anti-Mac-2, 1:300; Cerdalene Labs, Burlington, CA, USA); anti-Klotho (1:300; ABCAM); anti-proliferating cell nuclear antigen (anti-PCNA, 1:1000; ABCAM); and anti-adiponectin (1:300; ABCAM). The reaction product was detected with a horseradish peroxidase-conjugated system (anti-rabbit polymer; Dako, Glostrup, Denmark), and the color reaction was developed with 3,3-diaminobenzidine (Sigma-Aldrich). The histological sections for PCNA and Mac-2 were divided into 25 fields (0.087 mm² each; magnification, × 400), in which cells were counted, and the counts are expressed as cells/0.087mm². Expression of adiponectin and Klotho was quantified by using a point grid overlaid onto the microscopy image. The result is expressed as the proportion of positively immunostained cells.

da Silva I.O., de Menezes N.K., Jacobina H.D., Parra A.C., Souza F.L., Castro L.C., Roelofs J.J., Tammaro A., Gomes S.A., Sanches T.R, & Andrade L. (2024). Obesity aggravates acute kidney injury resulting from ischemia and reperfusion in mice. Scientific Reports, 14, 9820.

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Western Blot Analysis of Melanocyte Signaling

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Cultured primary melanocytes were lysed at 4°C in cell lysis buffer (50 mmol/L Tris pH 8.0, 150 mmol/L NaCl, 50 mmol/L EDTA, 0.5% NP-40) supplemented with a protease inhibitor cocktail (Roche). After SDS-PAGE, lysates were transferred to PVDF membranes (Millipore). Membrane blocking (5% milk in TBS, 0.2% Tween-20) was followed by incubation with the appropriate primary antibodies and HRP-conjugated secondary antibody (Cell Signaling Technology). Proteins were detected with the ECL substrate or the SuperSignal West Pico Chemiluminescent Substrate (Thermo Fisher Scientific). The primary antibodies used were as follows: anti-ERK2 (Santa Cruz Biotechnology Inc.), anti–p-ERk, anti–phospho-Akt (Ser473), anti-Akt (Cell Signaling Technology), anti-cyclin A (Santa Cruz Biotechnology), anti-PCNA (Abcam), and anti-actin (Sigma).

Bonvin E., Radaelli E., Bizet M., Luciani F., Calonne E., Putmans P., Nittner D., Singh N.K., Santagostino S.F., Petit V., Larue L., Marine J.C, & Fuks F. (2018). Tet2-dependent Hydroxymethylome Plasticity Reduces Melanoma Initiation and Progression. Cancer research, 79(3), 482-494.

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Western Blot Analysis of Vascular Proteins

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Total protein of cells and vascular tissues was extracted with protein lysis buffer (Beyotime, China) and protease inhibitor mix (Thermo Fisher Scientific, USA). A BCA kit (Thermo Fisher Scientific, USA) was used for protein quantification. The protein extract denatured at 98°C was then separated by 10% SDS-PAGE, transferred to a 0.4 μm pore size PVDF membrane and blocked in a 5% skim milk solution for 1 h at room temperature. After washing in TBST solution, the membranes were incubated overnight at 4°C in the following antibody solutions: anti-α-SMA (1:10,000; Proteintech, Cat# 55135-1-AP, China), anti-SMMHC (1:1,000; Proteintech, Cat# 21404-1AP), anti-CNN1 (1:1,000; Cell Signaling Technology, Cat# 17819, USA), anti-PCNA (1:10,000; Abcam, Cat# ab92552, USA), anti-CBX3 (1:1,000; Proteintech, Cat #11650-2-AP), and anti-β-actin (1:1,000; Proteintech, Cat# 66009-1-Ig). On the following day, the membranes were washed and incubated in the corresponding secondary antibody solutions (1:10,000, EasyBio, China, Cat# BE0132-100) for 1 h at room temperature. An ECL Chemiluminescence Kit (Millipore, USA) was used to detect the protein signal. ImageJ was used for gray value analysis.

Rong Z., Li F., Zhang R., Niu S., Di X., Ni L, & Liu C. (2023). Inhibition of tiRNA-Gly-GCC ameliorates neointimal formation via CBX3-mediated VSMCs phenotypic switching. Frontiers in Cardiovascular Medicine, 10, 1030635.

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