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Anti pcna pc10

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Anti-PCNA (PC10) is a mouse monoclonal antibody that recognizes the Proliferating Cell Nuclear Antigen (PCNA) protein. PCNA is a nuclear protein involved in DNA replication and repair processes.

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Lab products found in correlation

Anti flag m2, by Merck Group (3 mentions) Anti fn antibody ab, by Merck Group (2 mentions) Anti apkc c 20 sc216, by Santa Cruz Biotechnology (2 mentions) Alexa fluor 488 or 546 phalloidin, by Thermo Fisher Scientific (2 mentions) Anti γh2ax jbw301, by Merck Group (2 mentions) Anti cox 4, by Abcam (1 mentions) Polyacrylamide gel, by Bio-Rad (1 mentions) Anti gapdh, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Anti actin, by Merck Group (1 mentions) Anti gfp, by Merck Group (1 mentions) Anti ki67 antibodies, by Merck Group (1 mentions) Anti chk1 g 4, by Santa Cruz Biotechnology (1 mentions) Normal mouse igg, by Santa Cruz Biotechnology (1 mentions) Anti flag m2 magnetic bead, by Merck Group (1 mentions) Anti fancd2, by Novus Biologicals (1 mentions) Aphidicolin, by Fujifilm (1 mentions) Cordycepin, by Fujifilm (1 mentions) Anti α tubulin t5168, by Merck Group (1 mentions) Anti fanca, by Fortis Life Sciences (1 mentions)

Spelling variants of this product

Anti-PCNA (145 citations) PCNA (PC10) (16 citations) Mouse anti-PCNA (PC10, (5 citations) Anti-PCNA (clone PC10, (4 citations) Anti-PCNA (PC10) antibody (2 citations)

8 protocols using anti pcna pc10

1

Mitochondrial Enzyme Profiling in Ercc1 Mice

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Liver and kidney samples from 18-week-old Ercc1−/Δ and WT mice (n = 5) were homogenized in RIPA buffer (Pierce, Rockford, IL) with protease inhibitor cocktail (Roche, Indianapolis, IN). Mitochondrial extracts were prepared using Mitochondria Isolation Kit (Pierce) per the manufacturer’s specifications. Samples were separated on 4–20% polyacrylamide gel (Bio-Rad, Hercules, CA), transferred to nitrocellulose membrane, blocked and blotted with anti-PCNA (PC10, Santa Cruz Biotechnology, Santa Cruz, CA), anti-ERCC1 (D-10, Santa Cruz Biotechnology), anti-COXIV (Abcam, Cambridge, MA), anti-XPF (SPM228, Novus Biologicals, Littleton, CO) or anti-GAPDH, anti-MnSOD, anti-CuZnSOD, anti-catalase (3H3L29), anti-XO, and anti-rabbit secondary (all from Life Technologies, Carlsbad, CA) then visualized with ECL reagent (Pierce). Films exposed to membrane were imaged with ImageJ (NIH, Bethesda, MD). GAPDH was used as a loading control.
Robinson A.R., Yousefzadeh M.J., Rozgaja T.A., Wang J., Li X., Tilstra J.S., Feldman C.H., Gregg S.Q., Johnson C.H., Skoda E.M., Frantz M.C., Bell-Temin H., Pope-Varsalona H., Gurkar A.U., Nasto L.A., Robinson R.A., Fuhrmann-Stroissnigg H., Czerwinska J., McGowan S.J., Cantu-Medellin N., Harris J.B., Maniar S., Ross M.A., Trussoni C.E., LaRusso N.F., Cifuentes-Pagano E., Pagano P.J., Tudek B., Vo N.V., Rigatti L.H., Opresko P.L., Stolz D.B., Watkins S.C., Burd C.E., Croix C.M., Siuzdak G., Yates N.A., Robbins P.D., Wang Y., Wipf P., Kelley E.E, & Niedernhofer L.J. (2018). Spontaneous DNA damage to the nuclear genome promotes senescence, redox imbalance and aging. Redox Biology, 17, 259-273.
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2

TRAIP Antibody Production and Validation

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The TRAIP polyclonal antibody was raised against GST-TRAIP-N terminal fusion protein (see Figure 3e) and affinity purified using column coated with MBP-TRAIP-N terminal fusion protein. Antibody specifically recognizing γH2AX was previously described [42 (link)]. The anti-PCNA (PC10) and anti-CHK1 (G-4) antibodies were from Santa Cruz (Dallas, TX, USA); anti-Ki67 antibodies were from Chemicon (Darmstadt, Germany); anti-RPA1 antibodies were from Calbiochem (Darmstadt, Germany); anti-Chk1-pS345 antibodies were from Cell Signaling (Danvers, MA, USA); anti-KAP1 antibodies were from BD Transduction Laboratories (San Jose, CA, USA). Anti-Actin, anti-GFP and anti-Flag (M2) antibodies were obtained from Sigma (Darmstadt, Germany). ATMi (KU55993) and ATRi (VE821) inhibitors were from SelleckChem (Houston, TX, USA).
Feng W., Guo Y., Huang J., Deng Y., Zang J, & Huen M.S. (2016). TRAIP regulates replication fork recovery and progression via PCNA. Cell Discovery, 2, 16016-.
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3

Cryosectioning and Immunostaining of Fixed Embryos

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Embryos were fixed in either 4% PFA, Dent fixative or 1% TCA for 1-3 days and subjected to cryosectioning as described previously31 (link). Antibodies used were: anti-FN antibody (Ab), Sigma F3648 at 1:100; β-integrin monoclonal Ab, 8c8 (Developmental Studies Hybridoma Bank, USA) at 1:10; anti-aPKC C-20 (SC216, Santa Cruz Biotech, USA) at 1:100; anti-PCNA (PC10, Santa Cruz Biotech, USA) at 1:500; anti-laminin (Ab-1, NeoMarkers, USA) at 1:100 and anti-ZO-136 (link) (gift from Dr M Itoh) at 1:1. Sections were counterstained with Alexa Fluor 488 or 546 Phalloidin (A12379, A22283, Invitrogen USA) at 1:250 and TO-PRO-3 (T3605, Invitrogen, USA) at 1:1000.
Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H., Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S., Miesfeld J.B., Link B.A., Senga T., Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H., Heisenberg C.P, & Furutani-Seiki M. (2015). YAP is essential for tissue tension to ensure vertebrate 3D body shape. Nature, 521(7551), 217-221.
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4

DNA Damage Response Pathway Assay

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The following antibodies were obtained from commercial sources: anti-DNA:RNA (S9.6, Kerafast); anti-DDDDK-tag (MBL); anti-FLAG (M2, Sigma-Aldrich); anti-FLAG M2 magnetic beads (Sigma); normal mouse IgG (Santa Cruz); anti-FANCA (Bethyl); anti-FANCD2 (Novus); anti-PCNA (PC10, Santa Cruz); anti-γH2AX (JBW301, Millipore); anti-RPA (9H8, Abcam); anti-a-tubulin (T5168, Sigma). Aphidicolin (Wako), mitomycin C (MMC) (Kyowa Hakko Kirin), or cordycepin (Wako) were used at the indicated concentrations. Primers and siRNA oligos are summarized in Supplemental Table S1.
Okamoto Y., Iwasaki W.M., Kugou K., Takahashi K.K., Oda A., Sato K., Kobayashi W., Kawai H., Sakasai R., Takaori-Kondo A., Yamamoto T., Kanemaki M.T., Taoka M., Isobe T., Kurumizaka H., Innan H., Ohta K., Ishiai M, & Takata M. (2018). Replication stress induces accumulation of FANCD2 at central region of large fragile genes. Nucleic Acids Research, 46(6), 2932-2944.
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5

Antibody-based Western Blot Analysis Protocol

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Antibodies used for Western blot analysis included the following: anti-C1orf55/SDE2 (epitope: a.a. 318–410; Sigma-Aldrich), anti-GFP (JL-8, Clontech), anti-HA (6E2, Cell Signaling), anti-pCHK1 (S317, Cell Signaling), anti-Actin (Cell Signaling), anti-CDT1 (Cell Signaling), anti-Flag (M2, Sigma-Aldrich), anti-Tubulin (Sigma-Aldrich), Cyclin E (H-12, Santa Cruz), anti-PCNA (PC-10, Santa Cruz), anti-Vinculin (H-300, Santa Cruz), anti-GST (B-14, Santa Cruz), Cyclin A (H-432, Santa Cruz), anti-γH2AX (JBW301, Millipore), anti-CDT2 (Bethyl), anti-pRPA (S33, Bethyl), pKAP-1 (S824, Bethyl), anti-ORC2 (BD Pharmingen), and anti-MUS81 (MTA30 2G10/3, Abcam). Mitomycin C, camptothecin, hydroxyurea, cycloheximide, aphidicolin, and Z-Leu-Leu-Leu-al (MG132) were purchased from Sigma-Aldrich. Rucaparib (AG-014699) was purchased from Selleckchem. MLN4924, ubiquitin vinyl sulfone, and ubiquitin aldehyde were purchased from Boston Biochem. Drugs were used at the concentrations indicated in the figure legends.
Jo U., Cai W., Wang J., Kwon Y., D’Andrea A.D, & Kim H. (2016). PCNA-Dependent Cleavage and Degradation of SDE2 Regulates Response to Replication Stress. PLoS Genetics, 12(12), e1006465.
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6

Quantitative Analysis of PCNA in Bladder Cancer

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Bladder cancer cells were grown on glass bottom dishes and stained with anti-PCNA (PC10; Santa Cruz Biotechnology Inc) and Alexa Fluor 532 goat anti-mouse (Invitrogen, Carlsbad, CA, USA) antibodies and DRAQ5 (eBioscience, San Diego, CA) as described [15] (link). The relative intensities of PCNA in cytosol/nuclei were calculated using mean region of interest containing at least 400 pixels using the Zeiss LSM 510 software.
Gederaas O.A., Søgaard C.D., Viset T., Bachke S., Bruheim P., Arum C.J, & Otterlei M. (2014). Increased Anticancer Efficacy of Intravesical Mitomycin C Therapy when Combined with a PCNA Targeting Peptide. Translational Oncology, 7(6), 812-823.
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7

Protein Expression Analysis in Cell Lysates

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Samples were collected and placed on ice in a lysis solution [50 mM Tris–HCl (pH 8.0), 150 mM NaCl, 1 mM EDTA, 1% NP-40, 10% glycerol] containing 0.5% SDS and 2 mM PMSF with a protease inhibitor cocktail (Sigma P-8340, 1:100). Cellular proteins were resolved on a 12.5% SDS–PAGE gel. The membrane was incubated for 1 h at room temperature in 5% skim milk in PBS with 0.05% Tween-20 (PBST), and the membrane was probed with anti-PCNA PC10 (Ref # sc56; Santa Cruz), anti-alpha tubulin (Ref# MA1-80017; Thermo Fisher Scientific), anti-actin (Ref #MA1-744; Thermo Fisher Scientific), anti-Vinculin (clone 7F9, Ref# 14-9777-80; eBioscience), anti-AID (Ref #14-959-82; Thermo Fisher Scientific), anti-polη (Ref# ab17725; Abcam), anti-FancD2 (Ref# sc20022; Santa Cruz), anti-USP1 (Ref # ab108104Ref; Abcam), anti-Msh2 (Ref #A300-451A; Bethyl), and anti-Msh6 (Ref # A300-022A; Bethyl) antibodies. Immunoreactivity was detected using a horseradish peroxidase-conjugated secondary antibody.
Lerner L.K., Bonte D., Le Guillou M., Mohammad M.M., Kasraian Z., Sarasin A., Despras E, & Aoufouchi S. (2022). Expression of Constitutive Fusion of Ubiquitin to PCNA Restores the Level of Immunoglobulin A/T Mutations During Somatic Hypermutation in the Ramos Cell Line. Frontiers in Immunology, 13, 871766.
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8

Cryosectioning and Immunostaining of Fixed Embryos

Cited 1 time
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Embryos were fixed in either 4% PFA, Dent fixative or 1% TCA for 1-3 days and subjected to cryosectioning as described previously31 (link). Antibodies used were: anti-FN antibody (Ab), Sigma F3648 at 1:100; β-integrin monoclonal Ab, 8c8 (Developmental Studies Hybridoma Bank, USA) at 1:10; anti-aPKC C-20 (SC216, Santa Cruz Biotech, USA) at 1:100; anti-PCNA (PC10, Santa Cruz Biotech, USA) at 1:500; anti-laminin (Ab-1, NeoMarkers, USA) at 1:100 and anti-ZO-136 (link) (gift from Dr M Itoh) at 1:1. Sections were counterstained with Alexa Fluor 488 or 546 Phalloidin (A12379, A22283, Invitrogen USA) at 1:250 and TO-PRO-3 (T3605, Invitrogen, USA) at 1:1000.
Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H., Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S., Miesfeld J.B., Link B.A., Senga T., Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H., Heisenberg C.P, & Furutani-Seiki M. (2015). YAP is essential for tissue tension to ensure vertebrate 3D body shape. Nature, 521(7551), 217-221.
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