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Santa Cruz Biotechnology proliferating cell nuclear antigen pcna
Proliferating Cell Nuclear Antigen Pcna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/proliferating cell nuclear antigen pcna/product/Santa Cruz Biotechnology
Average 85 stars, based on 1 article reviews
Price from $9.99 to $1999.99
proliferating cell nuclear antigen pcna - by Bioz Stars, 2020-07
85/100 stars

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Related Articles

Western Blot:

Article Title: FKBP12, the 12-kDa FK506-binding protein, is a physiologic regulator of the cell cycle
Article Snippet: .. Protein (50 μg) was loaded in each well, SDS/PAGE was performed, and, after transfer to nitrocellulose paper, Western blots were performed at 1:500 dilution with antiserum to cyclin D1, p21, proliferating-cell nuclear antigen (PCNA), or actin (Santa Cruz Biotechnology) and a 1:2,000 dilution with anti-mouse horseradish peroxidase-coupled secondary antibody (DAKO). .. For phosphorylated p38 blots, cells were treated with TGF-β1 at 10 ng/ml for 30 min and lysed with lysis buffer A.

SDS Page:

Article Title: FKBP12, the 12-kDa FK506-binding protein, is a physiologic regulator of the cell cycle
Article Snippet: .. Protein (50 μg) was loaded in each well, SDS/PAGE was performed, and, after transfer to nitrocellulose paper, Western blots were performed at 1:500 dilution with antiserum to cyclin D1, p21, proliferating-cell nuclear antigen (PCNA), or actin (Santa Cruz Biotechnology) and a 1:2,000 dilution with anti-mouse horseradish peroxidase-coupled secondary antibody (DAKO). .. For phosphorylated p38 blots, cells were treated with TGF-β1 at 10 ng/ml for 30 min and lysed with lysis buffer A.

Mass Spectrometry:

Article Title: Human Cytomegalovirus Infection Leads to Accumulation of Geminin and Inhibition of the Licensing of Cellular DNA Replication
Article Snippet: .. The sources of the antibodies used were as follows: Orc1 (MS-649-P0; Neomarkers), Cdc6 (SC-9964; Santa Cruz Biotechnology), Mcm2 (68676E; BD Pharmingen), Mcm3 (68686E; BD Pharmingen), Mcm4 (68696E; BD Pharmingen), Mcm5 (68706E; BD Pharmingen), Mcm6 (68716E; BD Pharmingen), Mcm7 (MS-862-P0; NeoMarkers), lamins A/C (SC-7292; Santa Cruz Biotechnology), proliferating-cell nuclear antigen (PCNA) (SC-56; Santa Cruz Biotechnology), Dbf4 (SC-11354; Santa Cruz Biotechnology), and acetylated histone H3 (06-599; Upstate Biotech). .. The antibody against Cdt1 was a kind gift from Hideo Nishitani (Graduate School of Medical Science, Kyushu University, Kyushu, Japan), and the antibody against geminin was a kind gift from Anindya Dutta (Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Mass.).

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    Santa Cruz Biotechnology anti pcna
    The effects of cudratricusxanthone A ( 1 ) on IκB-α phosphorylation and degradation ( A ); NF-κB translocation ( B , C ); NF-κB localization as determined by immunofluorescence analysis ( D ); and NF-κB DNA binding activity ( E ) in BV2 microglia. Cells were pretreated for 3 h with the indicated concentrations of cudratricusxanthone A ( 1 ), and stimulated for 1 h with LPS (1 μg/mL). The LPS treatment was performed in the presence of compound. Western blot analyses of IκB-α and p -IκB-α in the cytoplasm ( A ) and NF-κB in the cytoplasm ( B ) and nucleus ( C ) and immunofluorescence analyses ( E ) were carried out as described in the Experimental Section. The band intensity was quantified by densitometry and normalized to <t>β-actin</t> and <t>PCNA,</t> and the values are presented at the bottom of the each band. Relative data represent the means ± SDs of three experiments. * p
    Anti Pcna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 283 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti pcna/product/Santa Cruz Biotechnology
    Average 94 stars, based on 283 article reviews
    Price from $9.99 to $1999.99
    anti pcna - by Bioz Stars, 2020-07
    94/100 stars
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    93
    Santa Cruz Biotechnology cell nuclear antigen pcna
    Renal structure in diabetic mice in the presence and absence of Nox-4 inhibition. PAS staining (A, B,C) and immunohistochemistry for <t>PCNA</t> (D,E,F) showing that <t>STZ-induced</t> C57BL/6J mice have increased mesangial matrix, mild glomerulosclerosis and separation of tubules with tubular dilatation (B) in addition to increased proliferation (E) compared to control (A and D). Plumbagin (2 mg/kg/day) administration blocked diabetic induced effects (C and F). Proportion of area immunostained for PAS and PCNA is shown in (G and H) respectively. STZ and plumbagin were administered as described in the Material and Methods. Negative IgG was performed to confirm staining specificity (not shown). Magnification x 400.
    Cell Nuclear Antigen Pcna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 102 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell nuclear antigen pcna/product/Santa Cruz Biotechnology
    Average 93 stars, based on 102 article reviews
    Price from $9.99 to $1999.99
    cell nuclear antigen pcna - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    91
    Santa Cruz Biotechnology rabbit anti pcna
    Effects of CYP-treatment on AR, <t>Erα,</t> and <t>Pcna</t> in mLTC-1cells. (A) The mRNA levels of AR , ERα , and Pcna in mLTC-1 cells. (B) The protein levels of AR, Erα, and Pcna in mLTC-1 cells. (C) Quantitative analysis of scanning densitometry of protein levels from (B). The mRNA and protein levels of AR were downregulated after CYP treatment, which is consistent with the T levels. In contrast, the ERα mRNA and protein levels were upregulated. The Pcna mRNA and protein levels suggest that CYP treatment may promote the proliferation of Leydig cells. The data represent the mean ± SEM. * P
    Rabbit Anti Pcna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti pcna/product/Santa Cruz Biotechnology
    Average 91 stars, based on 17 article reviews
    Price from $9.99 to $1999.99
    rabbit anti pcna - by Bioz Stars, 2020-07
    91/100 stars
      Buy from Supplier

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    The effects of cudratricusxanthone A ( 1 ) on IκB-α phosphorylation and degradation ( A ); NF-κB translocation ( B , C ); NF-κB localization as determined by immunofluorescence analysis ( D ); and NF-κB DNA binding activity ( E ) in BV2 microglia. Cells were pretreated for 3 h with the indicated concentrations of cudratricusxanthone A ( 1 ), and stimulated for 1 h with LPS (1 μg/mL). The LPS treatment was performed in the presence of compound. Western blot analyses of IκB-α and p -IκB-α in the cytoplasm ( A ) and NF-κB in the cytoplasm ( B ) and nucleus ( C ) and immunofluorescence analyses ( E ) were carried out as described in the Experimental Section. The band intensity was quantified by densitometry and normalized to β-actin and PCNA, and the values are presented at the bottom of the each band. Relative data represent the means ± SDs of three experiments. * p

    Journal: Molecules

    Article Title: A Prenylated Xanthone, Cudratricusxanthone A, Isolated from Cudrania tricuspidata Inhibits Lipopolysaccharide-Induced Neuroinflammation through Inhibition of NF-κB and p38 MAPK Pathways in BV2 Microglia

    doi: 10.3390/molecules21091240

    Figure Lengend Snippet: The effects of cudratricusxanthone A ( 1 ) on IκB-α phosphorylation and degradation ( A ); NF-κB translocation ( B , C ); NF-κB localization as determined by immunofluorescence analysis ( D ); and NF-κB DNA binding activity ( E ) in BV2 microglia. Cells were pretreated for 3 h with the indicated concentrations of cudratricusxanthone A ( 1 ), and stimulated for 1 h with LPS (1 μg/mL). The LPS treatment was performed in the presence of compound. Western blot analyses of IκB-α and p -IκB-α in the cytoplasm ( A ) and NF-κB in the cytoplasm ( B ) and nucleus ( C ) and immunofluorescence analyses ( E ) were carried out as described in the Experimental Section. The band intensity was quantified by densitometry and normalized to β-actin and PCNA, and the values are presented at the bottom of the each band. Relative data represent the means ± SDs of three experiments. * p

    Article Snippet: Primary antibodies, including mouse/goat/rabbit anti-COX-2, anti-iNOS, anti-β-actin, anti-IкB-α, anti-phospho-IкB-α, anti-p50, anti-p65, and anti-PCNA, and secondary antibodies were purchased from Santa Cruz Biotechnology (Heidelberg, Germany).

    Techniques: Translocation Assay, Immunofluorescence, Binding Assay, Activity Assay, Western Blot

    Co-immunoprecipitation of XRCC1 and PCNA. ( A ) Anti-PCNA antibody pulls down XRCC1. Whole cell extracts prepared from human 293T cells were subject to immunoprecipitation with anti-PCNA antibody as described in Materials and Methods. The precipitated proteins (IP) were fractionated by SDS–PAGE and probed with either anti-XRCC1 or anti-PCNA antibodies (as indicated) using standard immunoblotting techniques. XRCC1, purified recombinant XRCC1; PCNA, purified recombinant PCNA; beads, agarose bead control, without PCNA antibody; WCE, whole cell extract (∼30 µg); IP, immunoprecipitant. ( B ) Anti-GFP antibody pulls down XRCC1–EYFP and PCNA. Cell extracts were prepared from HeLa cells stably expressing either XRCC1–EYFP or EYFP alone (EYFP-C1) and immunoprecipitations were performed with anti-GFP as described in Materials and Methods. The precipitated proteins (IP) were analyzed as above with the indicated antibodies. Input was 20% of the starting material from the XRCC1–EYFP extracts. Note that GFP alone is not shown, as it migrated at a much lower molecular weight than the XRCC1–EYFP fusion protein.

    Journal: Nucleic Acids Research

    Article Title: XRCC1 co-localizes and physically interacts with PCNA

    doi: 10.1093/nar/gkh556

    Figure Lengend Snippet: Co-immunoprecipitation of XRCC1 and PCNA. ( A ) Anti-PCNA antibody pulls down XRCC1. Whole cell extracts prepared from human 293T cells were subject to immunoprecipitation with anti-PCNA antibody as described in Materials and Methods. The precipitated proteins (IP) were fractionated by SDS–PAGE and probed with either anti-XRCC1 or anti-PCNA antibodies (as indicated) using standard immunoblotting techniques. XRCC1, purified recombinant XRCC1; PCNA, purified recombinant PCNA; beads, agarose bead control, without PCNA antibody; WCE, whole cell extract (∼30 µg); IP, immunoprecipitant. ( B ) Anti-GFP antibody pulls down XRCC1–EYFP and PCNA. Cell extracts were prepared from HeLa cells stably expressing either XRCC1–EYFP or EYFP alone (EYFP-C1) and immunoprecipitations were performed with anti-GFP as described in Materials and Methods. The precipitated proteins (IP) were analyzed as above with the indicated antibodies. Input was 20% of the starting material from the XRCC1–EYFP extracts. Note that GFP alone is not shown, as it migrated at a much lower molecular weight than the XRCC1–EYFP fusion protein.

    Article Snippet: As shown in Figure A, anti-PCNA antibody pulled down both PCNA and XRCC1 (see lane IP).

    Techniques: Immunoprecipitation, SDS Page, Purification, Recombinant, Stable Transfection, Expressing, Molecular Weight

    XRCC1 physically interacts with PCNA in vitro . Purified recombinant XRCC1 protein (+ lanes) was examined for physical association with purified recombinant POLβ, APE1, FEN1 or PCNA (as indicated) using the in vitro protein interaction assay described in Materials and Methods. Non-specific interactions of the four recombinant proteins with the affinity matrix were examined in the absence of XRCC1 (– lanes). Matrix bound proteins were analyzed by SDS–PAGE and silver staining (representative gel shown). I indicates the initial input for the POLβ, APE1, FEN1 and PCNA proteins. The asterisk denotes the location of the PCNA protein and the arrow indicates the position of the HIS- and S-tagged recombinant XRCC1 protein. Molecular weight protein standards are shown (in kDa) to the right.

    Journal: Nucleic Acids Research

    Article Title: XRCC1 co-localizes and physically interacts with PCNA

    doi: 10.1093/nar/gkh556

    Figure Lengend Snippet: XRCC1 physically interacts with PCNA in vitro . Purified recombinant XRCC1 protein (+ lanes) was examined for physical association with purified recombinant POLβ, APE1, FEN1 or PCNA (as indicated) using the in vitro protein interaction assay described in Materials and Methods. Non-specific interactions of the four recombinant proteins with the affinity matrix were examined in the absence of XRCC1 (– lanes). Matrix bound proteins were analyzed by SDS–PAGE and silver staining (representative gel shown). I indicates the initial input for the POLβ, APE1, FEN1 and PCNA proteins. The asterisk denotes the location of the PCNA protein and the arrow indicates the position of the HIS- and S-tagged recombinant XRCC1 protein. Molecular weight protein standards are shown (in kDa) to the right.

    Article Snippet: As shown in Figure A, anti-PCNA antibody pulled down both PCNA and XRCC1 (see lane IP).

    Techniques: In Vitro, Purification, Recombinant, Protein Interaction Assay, SDS Page, Silver Staining, Molecular Weight

    ( A ) Schematic of XRCC1 interacting regions and protein partners. Thus far, at least eight proteins (see text for details), including PCNA described in this work, have been found to directly interact with XRCC1. The regions that are responsible for these interactions, excluding PNK, have been assigned (see diagram). Note that TDP1 has not been shown to directly associate with XRCC1. ( B ). Also shown is lagging strand ligation.

    Journal: Nucleic Acids Research

    Article Title: XRCC1 co-localizes and physically interacts with PCNA

    doi: 10.1093/nar/gkh556

    Figure Lengend Snippet: ( A ) Schematic of XRCC1 interacting regions and protein partners. Thus far, at least eight proteins (see text for details), including PCNA described in this work, have been found to directly interact with XRCC1. The regions that are responsible for these interactions, excluding PNK, have been assigned (see diagram). Note that TDP1 has not been shown to directly associate with XRCC1. ( B ). Also shown is lagging strand ligation.

    Article Snippet: As shown in Figure A, anti-PCNA antibody pulled down both PCNA and XRCC1 (see lane IP).

    Techniques: Ligation

    Renal structure in diabetic mice in the presence and absence of Nox-4 inhibition. PAS staining (A, B,C) and immunohistochemistry for PCNA (D,E,F) showing that STZ-induced C57BL/6J mice have increased mesangial matrix, mild glomerulosclerosis and separation of tubules with tubular dilatation (B) in addition to increased proliferation (E) compared to control (A and D). Plumbagin (2 mg/kg/day) administration blocked diabetic induced effects (C and F). Proportion of area immunostained for PAS and PCNA is shown in (G and H) respectively. STZ and plumbagin were administered as described in the Material and Methods. Negative IgG was performed to confirm staining specificity (not shown). Magnification x 400.

    Journal: PLoS ONE

    Article Title: Plumbagin Ameliorates Diabetic Nephropathy via Interruption of Pathways that Include NOX4 Signalling

    doi: 10.1371/journal.pone.0073428

    Figure Lengend Snippet: Renal structure in diabetic mice in the presence and absence of Nox-4 inhibition. PAS staining (A, B,C) and immunohistochemistry for PCNA (D,E,F) showing that STZ-induced C57BL/6J mice have increased mesangial matrix, mild glomerulosclerosis and separation of tubules with tubular dilatation (B) in addition to increased proliferation (E) compared to control (A and D). Plumbagin (2 mg/kg/day) administration blocked diabetic induced effects (C and F). Proportion of area immunostained for PAS and PCNA is shown in (G and H) respectively. STZ and plumbagin were administered as described in the Material and Methods. Negative IgG was performed to confirm staining specificity (not shown). Magnification x 400.

    Article Snippet: In addition, STZ-induced mice have increased levels of proliferating cell nuclear antigen (PCNA) suggesting increased tubular cell proliferation ( ) vs control ( ).

    Techniques: Mouse Assay, Inhibition, Staining, Immunohistochemistry

    Effects of CYP-treatment on AR, Erα, and Pcna in mLTC-1cells. (A) The mRNA levels of AR , ERα , and Pcna in mLTC-1 cells. (B) The protein levels of AR, Erα, and Pcna in mLTC-1 cells. (C) Quantitative analysis of scanning densitometry of protein levels from (B). The mRNA and protein levels of AR were downregulated after CYP treatment, which is consistent with the T levels. In contrast, the ERα mRNA and protein levels were upregulated. The Pcna mRNA and protein levels suggest that CYP treatment may promote the proliferation of Leydig cells. The data represent the mean ± SEM. * P

    Journal: PLoS ONE

    Article Title: Maternal Cypermethrin Exposure during the Perinatal Period Impairs Testicular Development in C57BL Male Offspring

    doi: 10.1371/journal.pone.0096781

    Figure Lengend Snippet: Effects of CYP-treatment on AR, Erα, and Pcna in mLTC-1cells. (A) The mRNA levels of AR , ERα , and Pcna in mLTC-1 cells. (B) The protein levels of AR, Erα, and Pcna in mLTC-1 cells. (C) Quantitative analysis of scanning densitometry of protein levels from (B). The mRNA and protein levels of AR were downregulated after CYP treatment, which is consistent with the T levels. In contrast, the ERα mRNA and protein levels were upregulated. The Pcna mRNA and protein levels suggest that CYP treatment may promote the proliferation of Leydig cells. The data represent the mean ± SEM. * P

    Article Snippet: The membrane was incubated with mouse anti-β-Actin, rabbit anti-Star, goat anti-3β-HSD, rabbit anti-CYP17A1, goat anti-17β-HSD3, rabbit anti-Pcna, rabbit anti-AR, and rabbit anti-ERα (further information on the primary antibodies are shown in , purchased from Santa Cruz, USA).

    Techniques:

    3β-HSD, Pcna immunohistochemistry and TUNEL assay of testes. Slides of (A, B, C) control and (D, E, F) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively, were immunolocalized with antibody for 3β-HSD. Slides of (G, H, I) control and (J, K, L) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively, were immunolocalized with antibody for Pcna. Slides of (M, N, O) control and (P, Q, R) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively were stained using the TUNEL method. All of the images were taken at 400× magnification. Scale bars, 40 µm. (S) Quantification of 3β-HSD-positive Leydig cells in 5–20 related slides of A–F. (T) Quantification of Pcna-positive germ cells in 5–20 related slides of G–L. (U) Quantification of apoptotic germ cells in 5–20 related slides of M–R. The data represent the mean ± SEM. * P

    Journal: PLoS ONE

    Article Title: Maternal Cypermethrin Exposure during the Perinatal Period Impairs Testicular Development in C57BL Male Offspring

    doi: 10.1371/journal.pone.0096781

    Figure Lengend Snippet: 3β-HSD, Pcna immunohistochemistry and TUNEL assay of testes. Slides of (A, B, C) control and (D, E, F) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively, were immunolocalized with antibody for 3β-HSD. Slides of (G, H, I) control and (J, K, L) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively, were immunolocalized with antibody for Pcna. Slides of (M, N, O) control and (P, Q, R) CYP-treated offspring at PD21.5, PD45.5, and PD90.5, respectively were stained using the TUNEL method. All of the images were taken at 400× magnification. Scale bars, 40 µm. (S) Quantification of 3β-HSD-positive Leydig cells in 5–20 related slides of A–F. (T) Quantification of Pcna-positive germ cells in 5–20 related slides of G–L. (U) Quantification of apoptotic germ cells in 5–20 related slides of M–R. The data represent the mean ± SEM. * P

    Article Snippet: The membrane was incubated with mouse anti-β-Actin, rabbit anti-Star, goat anti-3β-HSD, rabbit anti-CYP17A1, goat anti-17β-HSD3, rabbit anti-Pcna, rabbit anti-AR, and rabbit anti-ERα (further information on the primary antibodies are shown in , purchased from Santa Cruz, USA).

    Techniques: Immunohistochemistry, TUNEL Assay, Staining

    Effects of maternal CYP-exposure on the AR, ERα, Pcna, and E2/T levels of offspring. (A) The mRNA level of AR was not affected at PD21.5. The ERα level was upregulated significantly in the 12 mg/kg/day-exposure group, and there was an increasing trend in the other exposure group. Pcna expression was not altered. (B) AR expression was downregulated significantly in the exposure groups, and ERα and Pcna were upregulated, which may explain the hyperplasia of interstitial cells. (C) AR and Pcna were downregulated significantly, and ERα was upregulated, as observed at PD21.5 and PD45.5. (D) Serum T and E 2 levels and the E 2 /T ratio at the three time points. The T level was lower, and the E 2 level was higher in the CYP exposure groups at PD45.5 and PD90.5. The data represent the mean ± SEM. * P

    Journal: PLoS ONE

    Article Title: Maternal Cypermethrin Exposure during the Perinatal Period Impairs Testicular Development in C57BL Male Offspring

    doi: 10.1371/journal.pone.0096781

    Figure Lengend Snippet: Effects of maternal CYP-exposure on the AR, ERα, Pcna, and E2/T levels of offspring. (A) The mRNA level of AR was not affected at PD21.5. The ERα level was upregulated significantly in the 12 mg/kg/day-exposure group, and there was an increasing trend in the other exposure group. Pcna expression was not altered. (B) AR expression was downregulated significantly in the exposure groups, and ERα and Pcna were upregulated, which may explain the hyperplasia of interstitial cells. (C) AR and Pcna were downregulated significantly, and ERα was upregulated, as observed at PD21.5 and PD45.5. (D) Serum T and E 2 levels and the E 2 /T ratio at the three time points. The T level was lower, and the E 2 level was higher in the CYP exposure groups at PD45.5 and PD90.5. The data represent the mean ± SEM. * P

    Article Snippet: The membrane was incubated with mouse anti-β-Actin, rabbit anti-Star, goat anti-3β-HSD, rabbit anti-CYP17A1, goat anti-17β-HSD3, rabbit anti-Pcna, rabbit anti-AR, and rabbit anti-ERα (further information on the primary antibodies are shown in , purchased from Santa Cruz, USA).

    Techniques: Expressing