anti proliferating cell nuclear antigen pcna  (GeneTex)

 
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    Structured Review

    GeneTex anti proliferating cell nuclear antigen pcna
    Anti Proliferating Cell Nuclear Antigen Pcna, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti proliferating cell nuclear antigen pcna/product/GeneTex
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    anti proliferating cell nuclear antigen pcna - by Bioz Stars, 2020-07
    90/100 stars

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    Staining:

    Article Title: Erythrocytosis and Pulmonary Hypertension in a Mouse Model of Human HIF2A Gain of Function Mutation *
    Article Snippet: .. After deparaffinization/rehydration and antigen retrieval, the slides were stained with rabbit anti-smooth muscle α-actin (α-SMA) (1:500, Genetex catalog number 100034) or anti-proliferating cell nuclear antigen (PCNA) (1:200, Genetex catalog number 100539), biotinylated goat anti-rabbit antibody (1:200, BD Pharmingen), and streptavidin-horseradish peroxidase (BD Pharmingen). ..

    other:

    Article Title: Flavonoids from Gynostemma pentaphyllum Exhibit Differential Induction of Cell Cycle Arrest in H460 and A549 Cancer Cells
    Article Snippet: Anti-cyclin A and anti-proliferating cell nuclear antigen (PCNA) were from GeneTex Inc. (Irvine, CA, USA).

    Article Title: Early colonizing Escherichia coli elicits remodeling of rat colonic epithelium shifting toward a new homeostatic state
    Article Snippet: The following primary antibodies were used: anti-Ki67 (DakoCytomation); anti-proliferating cell nuclear antigen (PCNA) (GeneTex, Irving, CA, USA), anti-KLF4 and anti-phospho-histone H3 (PH3) (Abcam, Cambridge, MA, USA); anti-cyclin A, anti-p21CIP1 , anti-p27KIP1 , anti-MUC2, anti-Bax, anti-carbonic anhydrase II (CAII) (Santa Cruz Biotechnology, Dallas, TX, USA); anti-ZO-1, anti-claudin-1, anti-occludin (Invitrogen, Saint Aubin, France).

    Article Title: A low-salt diet increases the expression of renal sirtuin 1 through activation of the ghrelin receptor in rats
    Article Snippet: The primary antibodies included anti-Sirt1 (1:250 in glomerular cytoplasmic and nuclear fraction samples, and 1:1000 in others; Sigma-Aldrich), anti-β-actin (1:10000; Cell Signaling Technology, Danvers, MA), anti-proliferating cell nuclear antigen (PCNA), anti-Lamin A/C (both 1:1000; GeneTex Inc., Irvine, CA), anti-ghrelin (1:500; Santa Cruz Biotechnology Inc.), and anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (1:2000; GenScript, Piscataway, NJ).

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    GeneTex cell nuclear antigen pcna
    Immunostaining of <t>PCNA</t> in murine endometrial implants. PCNA immunostainingwas carried out on endometrial implants from KO/KO mice (A), WT/WT mice (B) and mice treated with ISO-1 (C) or rhMIF (D). Insets show general histological views of endometrial implants. Black arrows show <t>CD74</t> positive cells. Scale bar,10 µm.
    Cell Nuclear Antigen Pcna, supplied by GeneTex, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell nuclear antigen pcna/product/GeneTex
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cell nuclear antigen pcna - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    92
    GeneTex antibodies against pcna
    LPS modulated cell proliferation and apoptosis in embryonic chick lungs. (A, B, C): In immunofluorescent staining of chick lungs, red color shows <t>PCNA,</t> green color shows <t>pHIS3</t> and blue color shows DAPI staining, respectively. The far right panel indicates the dotted squares of the merged images with higher magnification. Compared to control, PCNA and pHIS3 expression were down-regulated in E14, while up-regulated in E18 chick lungs upon LPS exposure, respectively. (D, E): TUNEL staining of E14 and E18 chick lungs, respectively. The right panels indicate the dotted squares with higher magnification. LPS reduced TUNEL + cells in E14 and E18 chick lungs, respectively. (F): qPCR data show LPS induced up-regulation of cell cycle related gene expressions in E18 lungs. *PÂÂ
    Antibodies Against Pcna, supplied by GeneTex, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against pcna/product/GeneTex
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    antibodies against pcna - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    92
    GeneTex pcna
    EBV infection is associated with bivalent histone modification of members of the BER pathway independent of promoter hypermethylation. ( A and B ) The real-time qPCR validated the down-regulation of the seven BER candidate genes in the EBV-infected NPE cells, and the down-regulation was observed in the 18 paired NPC biopsies. Reduced expression of APEX , POLB , <t>PCNA</t> , TDG , and OGG1 is statistically significant ( P
    Pcna, supplied by GeneTex, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pcna/product/GeneTex
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pcna - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    Image Search Results


    Immunostaining of PCNA in murine endometrial implants. PCNA immunostainingwas carried out on endometrial implants from KO/KO mice (A), WT/WT mice (B) and mice treated with ISO-1 (C) or rhMIF (D). Insets show general histological views of endometrial implants. Black arrows show CD74 positive cells. Scale bar,10 µm.

    Journal: PLoS ONE

    Article Title: Macrophage Migration Inhibitory Factor Is Involved in Ectopic Endometrial Tissue Growth and Peritoneal-Endometrial Tissue Interaction In Vivo: A Plausible Link to Endometriosis Development

    doi: 10.1371/journal.pone.0110434

    Figure Lengend Snippet: Immunostaining of PCNA in murine endometrial implants. PCNA immunostainingwas carried out on endometrial implants from KO/KO mice (A), WT/WT mice (B) and mice treated with ISO-1 (C) or rhMIF (D). Insets show general histological views of endometrial implants. Black arrows show CD74 positive cells. Scale bar,10 µm.

    Article Snippet: To detect CD74, MIF receptor, and proliferating cell nuclear antigen (PCNA), sections were incubated for 90 min at room temperature with a rabbit polyclonal anti-human CD74 (GeneTex, Irvine, Canada) [1∶1600 dilution in PBS/bovine serum albumin (BSA) 0.02%/Tween-20 0.05%] or a rabbit polyclonal anti-human PCNA (GeneTex, Irvine, Canada) [1∶800 dilution in PBS/bovine serum albumin (BSA) 0.02%/Tween-20 0.05%].

    Techniques: Immunostaining, Mouse Assay

    LPS modulated cell proliferation and apoptosis in embryonic chick lungs. (A, B, C): In immunofluorescent staining of chick lungs, red color shows PCNA, green color shows pHIS3 and blue color shows DAPI staining, respectively. The far right panel indicates the dotted squares of the merged images with higher magnification. Compared to control, PCNA and pHIS3 expression were down-regulated in E14, while up-regulated in E18 chick lungs upon LPS exposure, respectively. (D, E): TUNEL staining of E14 and E18 chick lungs, respectively. The right panels indicate the dotted squares with higher magnification. LPS reduced TUNEL + cells in E14 and E18 chick lungs, respectively. (F): qPCR data show LPS induced up-regulation of cell cycle related gene expressions in E18 lungs. *PÂÂ

    Journal: Cell Cycle

    Article Title: Oxidative stress and NF-κB signaling are involved in LPS induced pulmonary dysplasia in chick embryos

    doi: 10.1080/15384101.2018.1496743

    Figure Lengend Snippet: LPS modulated cell proliferation and apoptosis in embryonic chick lungs. (A, B, C): In immunofluorescent staining of chick lungs, red color shows PCNA, green color shows pHIS3 and blue color shows DAPI staining, respectively. The far right panel indicates the dotted squares of the merged images with higher magnification. Compared to control, PCNA and pHIS3 expression were down-regulated in E14, while up-regulated in E18 chick lungs upon LPS exposure, respectively. (D, E): TUNEL staining of E14 and E18 chick lungs, respectively. The right panels indicate the dotted squares with higher magnification. LPS reduced TUNEL + cells in E14 and E18 chick lungs, respectively. (F): qPCR data show LPS induced up-regulation of cell cycle related gene expressions in E18 lungs. *PÂÂ

    Article Snippet: After being immersed in 3% hydrogen peroxide for 10 min to block endogenous peroxidase, the sections were blocked with 5% inactivated goat serum for 30 min at room temperature and incubated with primary antibodies against PCNA (1:300; GeneTex), pHIS3 (1:200; Santa Cruz), CAV-1 (1:200; Thermo Scientific), AQP5 (1:100; Abcam), Collagen І (1:200; Abcam), P65 (1:200; Sigma), Nrf2 (1:20; DSHB) and GATA-6 (1:300; Abcam), respectively, at 4°C overnight with shaking.

    Techniques: Staining, Expressing, TUNEL Assay, Real-time Polymerase Chain Reaction

    Methylation of FEN1 ensures its interaction with PCNA via suppression of its phosphorylation ( a ) Methylated FEN1 is resistant to phosphorylation and forms a complex with PCNA. Methylated or non-methylated FEN1 were incubated with Cdk2/Cyclin E followed by pull-down with PCNA-beads. Bound proteins were analyzed by anti-FEN1 or anti-PCNA antibodies. ( b ) In vitro phosphorylation and PCNA binding assay of WT and FEN1 mutants. WT or mutant FEN1 proteins, with or without phosphorylation, were subjected to PCNA beads. Phosphorylation of FEN1 was analyzed by autoradiography and the pulled-down proteins were immunodetected by anti-FEN1 and anti-PCNA antibodies. ( c ) Co-localization of FEN-1 and PCNA in S-phase cells. Cells were fixed and co-stained with anti-FEN-1 and anti-PCNA antibodies. ( d ) Co-localization of FEN-1 and BrdU in cells in S phase. Cells were labeled (1 h) with BrdU, followed by fixation and co-staining with anti-FEN-1 and anti-BrdU antibodies. Scale bars, 10 μm. For the full image, see Supplementary Figure 10 .

    Journal: Nature chemical biology

    Article Title: Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding

    doi: 10.1038/nchembio.422

    Figure Lengend Snippet: Methylation of FEN1 ensures its interaction with PCNA via suppression of its phosphorylation ( a ) Methylated FEN1 is resistant to phosphorylation and forms a complex with PCNA. Methylated or non-methylated FEN1 were incubated with Cdk2/Cyclin E followed by pull-down with PCNA-beads. Bound proteins were analyzed by anti-FEN1 or anti-PCNA antibodies. ( b ) In vitro phosphorylation and PCNA binding assay of WT and FEN1 mutants. WT or mutant FEN1 proteins, with or without phosphorylation, were subjected to PCNA beads. Phosphorylation of FEN1 was analyzed by autoradiography and the pulled-down proteins were immunodetected by anti-FEN1 and anti-PCNA antibodies. ( c ) Co-localization of FEN-1 and PCNA in S-phase cells. Cells were fixed and co-stained with anti-FEN-1 and anti-PCNA antibodies. ( d ) Co-localization of FEN-1 and BrdU in cells in S phase. Cells were labeled (1 h) with BrdU, followed by fixation and co-staining with anti-FEN-1 and anti-BrdU antibodies. Scale bars, 10 μm. For the full image, see Supplementary Figure 10 .

    Article Snippet: Antibodies The following antibodies were used: anti-FEN1 and anti-PCNA (GeneTex), anti-γH2AX and anti-mono methyl arginine (Abcam), anti-PhosSer, anti-asymmetric dimethyl-arginine and anti-symmetric dimethyl-arginine antibodies (Millipore), anti-Myc (sc-33) (Santa Cruz Biotechnologies), anti-PRMT5 (IMG 505) and anti-PRMT7 (IMG 512A) (Imgenex), anti-phosphor-Histone H3 (S10) and anti-α/β tubulin (Cell Signaling Technology), and anti-BrdU (Becton Dickinson).

    Techniques: Methylation, Incubation, In Vitro, Binding Assay, Mutagenesis, Autoradiography, Staining, Labeling

    Methylation of FEN1 is induced by H 2 O 2 and important for DNA repair H 2 O 2 treatment induces FEN1 methylation ( a ) and drives FEN1 to the nucleus from the cytoplasm ( b ). ( c-d ) LP-BER assay using cell extracts. Tetrahydrofuran-containing substrates (THF, top panel, circle), were incubated with indicated amounts of cell extract, followed by autoradiography (middle panel) and quantification (bottom panel). Unlabeled substrate and hot dCTP were used in ( c ) while nicked substrate with 3′-end label on the TFH-containing oligo and cold dNTP mixture were used in ( d ). ( e ) 4RK cells are sensitive to H 2 O 2 stress. HeLa cells (WT or 4RK) were treated (1 h) at indicated concentrations and cellular sensitivity was determined by growth inhibition experiments; mean ± s.d., n=4. ( f ) Spontaneous mutation frequency was evaluated with an Hprt mutant assay. ( g ) Model for FEN1 dynamic interaction with PCNA and DNA substrates regulated by FEN1 methylation and phosphorylation. Upon formation of flap structure in Okazaki fragment mutation or LP-BER, methylated FEN1 is recruited to the replication fork by interacting with PCNA, following the dissociation of Pol δ/β. Methylation of FEN1 ensures its interaction with and stimulation by PCNA to remove the flap structure. After DNA flap cleavage, FEN1 undergoes de-methylation and subsequent phosphorylation by cell cycle-dependent kinases, leading to disruption of the FEN1/PCNA interaction and dissociation of the nuclease from DNA substrates. Lig I is then recruited by interaction with PCNA and seals the nicks between two DNA fragments. For the full image, see Supplementary Figure 12 .

    Journal: Nature chemical biology

    Article Title: Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding

    doi: 10.1038/nchembio.422

    Figure Lengend Snippet: Methylation of FEN1 is induced by H 2 O 2 and important for DNA repair H 2 O 2 treatment induces FEN1 methylation ( a ) and drives FEN1 to the nucleus from the cytoplasm ( b ). ( c-d ) LP-BER assay using cell extracts. Tetrahydrofuran-containing substrates (THF, top panel, circle), were incubated with indicated amounts of cell extract, followed by autoradiography (middle panel) and quantification (bottom panel). Unlabeled substrate and hot dCTP were used in ( c ) while nicked substrate with 3′-end label on the TFH-containing oligo and cold dNTP mixture were used in ( d ). ( e ) 4RK cells are sensitive to H 2 O 2 stress. HeLa cells (WT or 4RK) were treated (1 h) at indicated concentrations and cellular sensitivity was determined by growth inhibition experiments; mean ± s.d., n=4. ( f ) Spontaneous mutation frequency was evaluated with an Hprt mutant assay. ( g ) Model for FEN1 dynamic interaction with PCNA and DNA substrates regulated by FEN1 methylation and phosphorylation. Upon formation of flap structure in Okazaki fragment mutation or LP-BER, methylated FEN1 is recruited to the replication fork by interacting with PCNA, following the dissociation of Pol δ/β. Methylation of FEN1 ensures its interaction with and stimulation by PCNA to remove the flap structure. After DNA flap cleavage, FEN1 undergoes de-methylation and subsequent phosphorylation by cell cycle-dependent kinases, leading to disruption of the FEN1/PCNA interaction and dissociation of the nuclease from DNA substrates. Lig I is then recruited by interaction with PCNA and seals the nicks between two DNA fragments. For the full image, see Supplementary Figure 12 .

    Article Snippet: Antibodies The following antibodies were used: anti-FEN1 and anti-PCNA (GeneTex), anti-γH2AX and anti-mono methyl arginine (Abcam), anti-PhosSer, anti-asymmetric dimethyl-arginine and anti-symmetric dimethyl-arginine antibodies (Millipore), anti-Myc (sc-33) (Santa Cruz Biotechnologies), anti-PRMT5 (IMG 505) and anti-PRMT7 (IMG 512A) (Imgenex), anti-phosphor-Histone H3 (S10) and anti-α/β tubulin (Cell Signaling Technology), and anti-BrdU (Becton Dickinson).

    Techniques: Methylation, Incubation, Autoradiography, Inhibition, Mutagenesis

    EBV infection is associated with bivalent histone modification of members of the BER pathway independent of promoter hypermethylation. ( A and B ) The real-time qPCR validated the down-regulation of the seven BER candidate genes in the EBV-infected NPE cells, and the down-regulation was observed in the 18 paired NPC biopsies. Reduced expression of APEX , POLB , PCNA , TDG , and OGG1 is statistically significant ( P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: EBV infection is associated with histone bivalent switch modifications in squamous epithelial cells

    doi: 10.1073/pnas.1821752116

    Figure Lengend Snippet: EBV infection is associated with bivalent histone modification of members of the BER pathway independent of promoter hypermethylation. ( A and B ) The real-time qPCR validated the down-regulation of the seven BER candidate genes in the EBV-infected NPE cells, and the down-regulation was observed in the 18 paired NPC biopsies. Reduced expression of APEX , POLB , PCNA , TDG , and OGG1 is statistically significant ( P

    Article Snippet: The antibodies, including APEX1 (1:1,000; Cell Signaling), POLB (1:1,000; GeneTex), POLD (1:1,000; GeneTex), PCNA (1:1,000, GeneTex), TDG (1:1,000, Abcam), OGG1 (1:1,000, Abcam), MLH1 (1:1,000; Cell Signaling), H3K4me3 (1:1,000; Cell Signaling), and total Histone H3 (1:10000; Cell Signaling), were used for detecting the expression of the targeted proteins, while p84 (1:1,000; GeneTex) was used as a loading control.

    Techniques: Infection, Modification, Real-time Polymerase Chain Reaction, Expressing