p27 Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Thermo Fisher anti p27
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    Anti P27, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p27/product/Thermo Fisher
    Average 90 stars, based on 38 article reviews
    Price from $9.99 to $1999.99
    anti p27 - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    85
    Becton Dickinson anti p 27
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    Anti P 27, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 85/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p 27/product/Becton Dickinson
    Average 85 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    anti p 27 - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    85
    Cell Signaling Technology Inc p 27 antibodies
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    P 27 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p 27 antibodies/product/Cell Signaling Technology Inc
    Average 85 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    p 27 antibodies - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    91
    Blackwell Publishing Inc p 27
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    P 27, supplied by Blackwell Publishing Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p 27/product/Blackwell Publishing Inc
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p 27 - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    89
    Santa Cruz Biotechnology anti p 27 antibody
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    Anti P 27 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p 27 antibody/product/Santa Cruz Biotechnology
    Average 89 stars, based on 54 article reviews
    Price from $9.99 to $1999.99
    anti p 27 antibody - by Bioz Stars, 2020-08
    89/100 stars
      Buy from Supplier

    91
    Lawrence Erlbaum Associates p 27
    Expression of BAP1 and cell cycle-related proteins. <t>P27</t> was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands
    P 27, supplied by Lawrence Erlbaum Associates, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p 27/product/Lawrence Erlbaum Associates
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p 27 - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    85
    Santa Cruz Biotechnology α p 27
    Spy1-enhanced proliferation is dependent on endogenous <t>p27.</t> (A) MEF–/– cells were transfected with the indicated constructs, medium was changed 24 h posttransfection, and cells were counted via trypan blue exclusion 48 h posttransfection. The graphed data indicate that exogenous p27 slows proliferation in the MEF–/– cells and that Spy1 can overcome this inhibition of proliferation. Spy1 does not enhance proliferation over mock control in cells lacking endogenous p27. The data are one representative experiment of four. Error bars indicate the SEM of three separate transfections. (B) Lysates were analyzed by 10% SDS-PAGE, transferred to nitrocellulose membrane, and immunoblotted with α-myc-Spy1, and <t>α-p27</t> sera to demonstrate protein expression. (C) Endogenous Spy1 was immunoprecipitated from either NIH3T3 cells null for p27 (3T3–/–) or NIH3T3 wt (3T3wt). Both lysate and immunoprecipitated samples were separated by 10% SDS-PAGE and immunoblotted with α-CDK2 sera (top panel) or α-p27 sera (bottom panel). (D) Endogenous CDK2 was immunoprecipitated from both 3T3wt and 3T3–/– cell types. Lysate samples and the immunoprecipitated samples were analyzed by 10% SDS-PAGE, and immunoblotting was carried out with α-Spy1 sera.
    α P 27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α p 27/product/Santa Cruz Biotechnology
    Average 85 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    α p 27 - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    99
    Cell Signaling Technology Inc p27
    JQ1 decreased MYC and elevated p21 protein abundance in human ATC cell lines. (ai) Immunohistochemical analysis for MYC protein was carried out after the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines were treated with vehicle or with JQ1 (500 nM) for 48 hours. (aii) Quantification of MYC-positive cells indicated reduction of MYC protein by JQ1. (bi–biv) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against MYC, p21, <t>p27,</t> cyclin D1, and CDK4 and the loading control α -tubulin, as described in the Materials and Methods section. (ci–civ) Band intensities in (b) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (di–div) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against p -Rb, total Rb, E2F-1, and E2F-3 and the loading control α -tubulin, as described in the Materials and Methods section. (ei–eiv) Band intensities in (di–div) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (fi–fiii) JQ1 inhibited cell cycle progression of ATC cell lines. (fi) Cell cycle profiles in THJ cell lines. The percentages of cell populations of different cell cycle phases are shown in the upper-right corner. After JQ1 treatments, all THJ cell lines were blocked in the G1/G0 phase, and there was reduction in the S and G2/M phases. (fii) JQ1 treatment lengthened the G1/G0 phase in ATC cells. (fiii) JQ1 treatment affected the distribution of cell cycle. Different cell cycle phases were quantified by 4′,6-diamidino-2-phenylindole staining, followed by fluorescence-activated cell sorting analysis in THJ cell lines.
    P27, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2469 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27/product/Cell Signaling Technology Inc
    Average 99 stars, based on 2469 article reviews
    Price from $9.99 to $1999.99
    p27 - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc anti p27
    PCBP1 up-regulates <t>p27</t> expression by enhancing the mRNA stability and translation. ( a ) Immunoblot of endogenous p27 protein levels upon transcription inhibition or/and proteasome degradation repression. A2780 cells overexpressing GFP-PCBP1 or GFP alone were treated with DMSO, Act D at 0.5 μg/ml for 8 h, MG132 at 20 μM for 4 h, or with their combination for 4 h, and analyzed. Results are representative of at least three independent experiments. ( b ) Immunoblot of endogenous p27 protein levels in A2780 cells with endogenous PCBP1 knockdown. Cells were treated with MG132 as in ( a ) ( c ) Immunoblot of p27 ubiquitin ligase Skp2 and p27 expression in the indicated cells. No evident Skp2 expression alteration is shown. ( d ) Immunoblot of the indicated proteins possibly related to p27 protein expression and cell survival. ( e ) Semi-quantitative RT-PCR analysis of p27 or c-myc mRNA stability in A2780 cells overexpressing PCBP1 or GFP control, on condition of Act D treatment to terminate the novel mRNA transcription. c-myc and GAPDH were used as positive and negative controls. The PCR of p27 were performed with 20 cycles, c-Myc with 25 and GAPDH for 20 cycles, respectively. Relative p27 and c-myc level against GAPDH were further normalized against DMSO treated GFP and shown at the bottom. ( f ) Semi-quantitative RT-PCR analyses of p27 or c-myc mRNA stability in A2780 cells with endogenous PCBP1 knockdown by specific shRNAs as the method in E. * p
    Anti P27, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 698 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p27/product/Cell Signaling Technology Inc
    Average 94 stars, based on 698 article reviews
    Price from $9.99 to $1999.99
    anti p27 - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    96
    Cell Signaling Technology Inc p27 kip1
    EL regulates the expression of G 1 -phase related genes. A549, H441, and H520 cells were treated with EL (100 μM) for 24 h. Relative mRNA expression levels for cyclin D1 , CDK2 , CDK4 , cdc25A , p21 WAF1/CIP1 , and <t>p27</t> <t>KIP1</t> were determined by quantitative
    P27 Kip1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 263 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27 kip1/product/Cell Signaling Technology Inc
    Average 96 stars, based on 263 article reviews
    Price from $9.99 to $1999.99
    p27 kip1 - by Bioz Stars, 2020-08
    96/100 stars
      Buy from Supplier

    92
    Santa Cruz Biotechnology p27
    E2F EMSAs. (A) The positions, directions, and sequences of the putative E2F sites of the rat, mouse, and human p27KIP1 promoters are depicted. The sequences of consensus E2F and E2F4-DP1 sites are indicated. The forward consensus sites are indicated by underlining, and the reverse consensus sites are indicated by bold and italics. Base pair numbers are relative to the translation start site for the <t>p27</t> protein. (B) EMSAs using control (Babe) and LMP1 nuclear lysates were performed. Complexes were competed with a 200-fold excess of consensus (comp) and mutant oligonucleotides. Supershifts with the indicated antibodies were performed. The arrow indicates the position of nonspecific complexes, and boxes highlight the positions of specific complexes. Arrowheads indicate the positions of the antibody-shifted complexes for E2F4 (closed arrowhead) and p130 (open arrowhead). Lane numbers are indicated below.
    P27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 3265 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27/product/Santa Cruz Biotechnology
    Average 92 stars, based on 3265 article reviews
    Price from $9.99 to $1999.99
    p27 - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    85
    Becton Dickinson anti p 27 monoclonal antibodies
    E2F EMSAs. (A) The positions, directions, and sequences of the putative E2F sites of the rat, mouse, and human p27KIP1 promoters are depicted. The sequences of consensus E2F and E2F4-DP1 sites are indicated. The forward consensus sites are indicated by underlining, and the reverse consensus sites are indicated by bold and italics. Base pair numbers are relative to the translation start site for the <t>p27</t> protein. (B) EMSAs using control (Babe) and LMP1 nuclear lysates were performed. Complexes were competed with a 200-fold excess of consensus (comp) and mutant oligonucleotides. Supershifts with the indicated antibodies were performed. The arrow indicates the position of nonspecific complexes, and boxes highlight the positions of specific complexes. Arrowheads indicate the positions of the antibody-shifted complexes for E2F4 (closed arrowhead) and p130 (open arrowhead). Lane numbers are indicated below.
    Anti P 27 Monoclonal Antibodies, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p 27 monoclonal antibodies/product/Becton Dickinson
    Average 85 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    anti p 27 monoclonal antibodies - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    92
    Thermo Fisher antibodies against p27
    Mitochondrial <t>p27</t> is sufficient to induce endothelial cell migration. (A, B) Endothelial cells were treated with 50 μM caffeine for 18 hours, and mitochondrial (“mito”) and nonmitochondrial (“non-mito”) fractions were separated. p27 and the closely related p21 protein were detected by immunoblot; TIM23 and Trx-1 served as purity controls for the fractions. (A) Representative immunoblots. (B) Semiquantitative analysis of mitochondrial p27 normalized to TIM23. Data are mean ± SEM, n = 6, * p
    Antibodies Against P27, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against p27/product/Thermo Fisher
    Average 92 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    antibodies against p27 - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    96
    Cell Signaling Technology Inc anti p27 kip1
    Cyclin‐dependent kinases and cyclins are involved in solute carrier family 35 member F2 ( SLC 35F2) ‐ regulated cell cycle progression. A, Effects of SLC 35F2 knockout on cell cycle by FACS . B, Cell cycle distribution showed that inhibition of SLC 35F2 induced cell cycle arrest at G1 phase. C, Flow cytometry analysis of the cell cycle of SLC 35F2 overexpression and empty vector control cells. D, Ectopic expression of SLC 35F2 promoted G1/S phase transition and increased S‐phase proportion. E, F, Protein levels of CDK 2, CDK 4, CDK 6, Cyclin D1, Cyclin D3, <t>p27</t> <t>Kip1,</t> p21 Waf1/Cip 1 and p18 INK 4C were detected by western blotting in indicated PTC cells. G, Relative mRNA expression levels of some cell cycle related genes analyzed by qPCR in SLC 35F2‐ KO group compared to control KTC ‐1 cells. Data were plotted relative to expression levels in control cells (* P
    Anti P27 Kip1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p27 kip1/product/Cell Signaling Technology Inc
    Average 96 stars, based on 93 article reviews
    Price from $9.99 to $1999.99
    anti p27 kip1 - by Bioz Stars, 2020-08
    96/100 stars
      Buy from Supplier

    92
    Horizon Discovery p27 si p27 id j 003472 05
    Cyclin‐dependent kinases and cyclins are involved in solute carrier family 35 member F2 ( SLC 35F2) ‐ regulated cell cycle progression. A, Effects of SLC 35F2 knockout on cell cycle by FACS . B, Cell cycle distribution showed that inhibition of SLC 35F2 induced cell cycle arrest at G1 phase. C, Flow cytometry analysis of the cell cycle of SLC 35F2 overexpression and empty vector control cells. D, Ectopic expression of SLC 35F2 promoted G1/S phase transition and increased S‐phase proportion. E, F, Protein levels of CDK 2, CDK 4, CDK 6, Cyclin D1, Cyclin D3, <t>p27</t> <t>Kip1,</t> p21 Waf1/Cip 1 and p18 INK 4C were detected by western blotting in indicated PTC cells. G, Relative mRNA expression levels of some cell cycle related genes analyzed by qPCR in SLC 35F2‐ KO group compared to control KTC ‐1 cells. Data were plotted relative to expression levels in control cells (* P
    P27 Si P27 Id J 003472 05, supplied by Horizon Discovery, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27 si p27 id j 003472 05/product/Horizon Discovery
    Average 92 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    p27 si p27 id j 003472 05 - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    91
    Beyotime p27 ap027
    Cyclin‐dependent kinases and cyclins are involved in solute carrier family 35 member F2 ( SLC 35F2) ‐ regulated cell cycle progression. A, Effects of SLC 35F2 knockout on cell cycle by FACS . B, Cell cycle distribution showed that inhibition of SLC 35F2 induced cell cycle arrest at G1 phase. C, Flow cytometry analysis of the cell cycle of SLC 35F2 overexpression and empty vector control cells. D, Ectopic expression of SLC 35F2 promoted G1/S phase transition and increased S‐phase proportion. E, F, Protein levels of CDK 2, CDK 4, CDK 6, Cyclin D1, Cyclin D3, <t>p27</t> <t>Kip1,</t> p21 Waf1/Cip 1 and p18 INK 4C were detected by western blotting in indicated PTC cells. G, Relative mRNA expression levels of some cell cycle related genes analyzed by qPCR in SLC 35F2‐ KO group compared to control KTC ‐1 cells. Data were plotted relative to expression levels in control cells (* P
    P27 Ap027, supplied by Beyotime, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27 ap027/product/Beyotime
    Average 91 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    p27 ap027 - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    88
    Santa Cruz Biotechnology p p27
    PHD3 depletion increases S10 phosphorylation of <t>p27</t> in hypoxia. a Western blot analysis of p27 expression in cells arrested at different cell cycle phases and exposed to PHD3 or control siRNA. PHD3 depletion has no effect on <t>T187</t> phosphorylation of p27 at any cell cycle phase. b PHD3 depletion has little effect on p27 phosphorylated on T157 and T198. c S10 phosphorylated form of p27 is strongly induced in PHD3 depleted cells. d Quantification of total and indicated p27 phosphoproteins from four independent experiments normalized to β-actin. Out of the phosphoproteins the effect on the expression of p27S10 is most prominent. Asterisk indicates significant difference ( p
    P P27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p p27/product/Santa Cruz Biotechnology
    Average 88 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    p p27 - by Bioz Stars, 2020-08
    88/100 stars
      Buy from Supplier

    p27  (Abcam)
    94
    Abcam p27
    Effect of lignans on expression of P21 and <t>P27</t> in RMCs induced by Ang II. β -actin and GAPDH were used as an internal loading control gene. Both mRNA and protein relative expression levels were expressed as folds of control. All values were expressed as mean ± SD ( n = 3). (a) Effect of lignans on mRNA expression of P21 and P27 by RT-qPCR. (b, c1~c2) Effect of lignans on protein expression of P21 and P27 by western blot; Con: control; Ang II: 10 −8 mol/L Ang II group; Epa: 10 −8 mol/L Ang II + 20 μ mol/L epalrestat group; L Lig: 10 −8 mol/L Ang II + 20 mg/L lignan group; M Lig: 10 −8 mol/L Ang II + 40 mg/L lignan group; H Lig: 10 −8 mol/L Ang II + 80 mg/L lignan group; ∗ P
    P27, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 498 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p27/product/Abcam
    Average 94 stars, based on 498 article reviews
    Price from $9.99 to $1999.99
    p27 - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    93
    Shanghai Genechem sh p27
    Effect of lignans on expression of P21 and <t>P27</t> in RMCs induced by Ang II. β -actin and GAPDH were used as an internal loading control gene. Both mRNA and protein relative expression levels were expressed as folds of control. All values were expressed as mean ± SD ( n = 3). (a) Effect of lignans on mRNA expression of P21 and P27 by RT-qPCR. (b, c1~c2) Effect of lignans on protein expression of P21 and P27 by western blot; Con: control; Ang II: 10 −8 mol/L Ang II group; Epa: 10 −8 mol/L Ang II + 20 μ mol/L epalrestat group; L Lig: 10 −8 mol/L Ang II + 20 mg/L lignan group; M Lig: 10 −8 mol/L Ang II + 40 mg/L lignan group; H Lig: 10 −8 mol/L Ang II + 80 mg/L lignan group; ∗ P
    Sh P27, supplied by Shanghai Genechem, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sh p27/product/Shanghai Genechem
    Average 93 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    sh p27 - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

    85
    Immunodiagnostics Inc sivmac251 p27
    Humoral immunity at the time of initial low-dose SHIV-1157ipEL-p challenge. (A) Reciprocal serum antibody ELISA titers against <t>SIVmac251</t> <t>p27</t> Gag, HIV-1 Tat and heterologous clade C HIV CN54 gp120. (B) NAb activity SHIV-1157ipEL-p and, SHIV SF162P4 ) and Tier 2 (SHIV-1157ipd3N4, SHIV-2873Nip) viruses was measured in human PBMC in the presence of polymyxin B. TZM-bl neutralization assay was also performed against SHIV-1157ipEL-p. IC 50 and IC 90 titers, reciprocal dilutions of serum giving 50% and 90% neutralization (inhibitory concentrations), respectively, are shown. *, Mamu A*001-positive RM.
    Sivmac251 P27, supplied by Immunodiagnostics Inc, used in various techniques. Bioz Stars score: 85/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sivmac251 p27/product/Immunodiagnostics Inc
    Average 85 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    sivmac251 p27 - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    85
    Santa Cruz Biotechnology c p27
    Humoral immunity at the time of initial low-dose SHIV-1157ipEL-p challenge. (A) Reciprocal serum antibody ELISA titers against <t>SIVmac251</t> <t>p27</t> Gag, HIV-1 Tat and heterologous clade C HIV CN54 gp120. (B) NAb activity SHIV-1157ipEL-p and, SHIV SF162P4 ) and Tier 2 (SHIV-1157ipd3N4, SHIV-2873Nip) viruses was measured in human PBMC in the presence of polymyxin B. TZM-bl neutralization assay was also performed against SHIV-1157ipEL-p. IC 50 and IC 90 titers, reciprocal dilutions of serum giving 50% and 90% neutralization (inhibitory concentrations), respectively, are shown. *, Mamu A*001-positive RM.
    C P27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c p27/product/Santa Cruz Biotechnology
    Average 85 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    c p27 - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    91
    Celltrion ct p27
    Humoral immunity at the time of initial low-dose SHIV-1157ipEL-p challenge. (A) Reciprocal serum antibody ELISA titers against <t>SIVmac251</t> <t>p27</t> Gag, HIV-1 Tat and heterologous clade C HIV CN54 gp120. (B) NAb activity SHIV-1157ipEL-p and, SHIV SF162P4 ) and Tier 2 (SHIV-1157ipd3N4, SHIV-2873Nip) viruses was measured in human PBMC in the presence of polymyxin B. TZM-bl neutralization assay was also performed against SHIV-1157ipEL-p. IC 50 and IC 90 titers, reciprocal dilutions of serum giving 50% and 90% neutralization (inhibitory concentrations), respectively, are shown. *, Mamu A*001-positive RM.
    Ct P27, supplied by Celltrion, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ct p27/product/Celltrion
    Average 91 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    ct p27 - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    88
    Santa Cruz Biotechnology si p27
    <t>p27</t> knockdown partially rescues MLN4924-induced migration and proliferation, but not tube formation MS1 cells were first transfected with siRNA targeting p27 and si-Cont for 72 hrs, followed by MLN4924 treatment for 24 hrs. One portion was subjected to IB ( A ), and the other portion was used for assays of migration ( B ), proliferation ( C ) and tube formation ( D ). Shown is mean ± SEM from three independent experiments. Scale bar represents 50 μm.
    Si P27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/si p27/product/Santa Cruz Biotechnology
    Average 88 stars, based on 45 article reviews
    Price from $9.99 to $1999.99
    si p27 - by Bioz Stars, 2020-08
    88/100 stars
      Buy from Supplier

    Image Search Results


    Expression of BAP1 and cell cycle-related proteins. P27 was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands

    Journal: BMC Cancer

    Article Title: BRCA1-associated protein 1 deficiency in lung adenocarcinoma predicts poor outcome and increased tumor invasion

    doi: 10.1186/s12885-016-2670-x

    Figure Lengend Snippet: Expression of BAP1 and cell cycle-related proteins. P27 was inversely influenced by BAP1 while CyclinB1 expression changed in accordance with BAP1. It is widely accepted that the expression of P27 is down-regulated when the cell cycle runs slower. MW is marked in red under the bands

    Article Snippet: Primary antibodies used were anti-GAPDH (#5632–1, Epitomics, Burlingame, CA, USA) as a loading control, anti-cyclinB1 (#4135, Cell Signaling, Boston, Massachusetts, USA), anti-P27 (kip1, #PA5–17830, Lab Vision Corporation, Fremont, CA) and anti-PARP-1 (#ab32138, Abcam, Massachusetts, USA).

    Techniques: Expressing

    Spy1-enhanced proliferation is dependent on endogenous p27. (A) MEF–/– cells were transfected with the indicated constructs, medium was changed 24 h posttransfection, and cells were counted via trypan blue exclusion 48 h posttransfection. The graphed data indicate that exogenous p27 slows proliferation in the MEF–/– cells and that Spy1 can overcome this inhibition of proliferation. Spy1 does not enhance proliferation over mock control in cells lacking endogenous p27. The data are one representative experiment of four. Error bars indicate the SEM of three separate transfections. (B) Lysates were analyzed by 10% SDS-PAGE, transferred to nitrocellulose membrane, and immunoblotted with α-myc-Spy1, and α-p27 sera to demonstrate protein expression. (C) Endogenous Spy1 was immunoprecipitated from either NIH3T3 cells null for p27 (3T3–/–) or NIH3T3 wt (3T3wt). Both lysate and immunoprecipitated samples were separated by 10% SDS-PAGE and immunoblotted with α-CDK2 sera (top panel) or α-p27 sera (bottom panel). (D) Endogenous CDK2 was immunoprecipitated from both 3T3wt and 3T3–/– cell types. Lysate samples and the immunoprecipitated samples were analyzed by 10% SDS-PAGE, and immunoblotting was carried out with α-Spy1 sera.

    Journal: Molecular Biology of the Cell

    Article Title: Spy1 Interacts with p27Kip1 to Allow G1/S Progression

    doi: 10.1091/mbc.E02-12-0820

    Figure Lengend Snippet: Spy1-enhanced proliferation is dependent on endogenous p27. (A) MEF–/– cells were transfected with the indicated constructs, medium was changed 24 h posttransfection, and cells were counted via trypan blue exclusion 48 h posttransfection. The graphed data indicate that exogenous p27 slows proliferation in the MEF–/– cells and that Spy1 can overcome this inhibition of proliferation. Spy1 does not enhance proliferation over mock control in cells lacking endogenous p27. The data are one representative experiment of four. Error bars indicate the SEM of three separate transfections. (B) Lysates were analyzed by 10% SDS-PAGE, transferred to nitrocellulose membrane, and immunoblotted with α-myc-Spy1, and α-p27 sera to demonstrate protein expression. (C) Endogenous Spy1 was immunoprecipitated from either NIH3T3 cells null for p27 (3T3–/–) or NIH3T3 wt (3T3wt). Both lysate and immunoprecipitated samples were separated by 10% SDS-PAGE and immunoblotted with α-CDK2 sera (top panel) or α-p27 sera (bottom panel). (D) Endogenous CDK2 was immunoprecipitated from both 3T3wt and 3T3–/– cell types. Lysate samples and the immunoprecipitated samples were analyzed by 10% SDS-PAGE, and immunoblotting was carried out with α-Spy1 sera.

    Article Snippet: The gels were then transferred to nitrocellulose membrane, immunoblotted with 1:2000 α-p27 (Santa Cruz Biotechnology, Santa Cruz, CA), 1:2000 α-CDK2, 1:4000 α-myc (9E10), 1:2000 α-flag (Sigma), or 1:500 α-Spy1 followed by ECL (Amersham, San Francisco, CA).

    Techniques: Transfection, Construct, Inhibition, SDS Page, Expressing, Immunoprecipitation

    Spy1 can overcome a p27-induced G 1 arrest. (A) NIH3T3 wild-type cells were transfected with the indicated constructs and treated with BrdU for 2 h. The cells were then fixed and examined by immunofluorescence for BrdU incorporation by examination of GFP-positive cells. The graphed data indicate that there is an increase in DNA synthesis when p27 and Spy1 are coexpressed in comparison to p27 alone. (B) The lysates from the BrdU experiment were analyzed by 10% SDS-PAGE; immunoblotting with α-flag, α-GFP, and α-p27 sera show approximately equivalent levels of protein expression.

    Journal: Molecular Biology of the Cell

    Article Title: Spy1 Interacts with p27Kip1 to Allow G1/S Progression

    doi: 10.1091/mbc.E02-12-0820

    Figure Lengend Snippet: Spy1 can overcome a p27-induced G 1 arrest. (A) NIH3T3 wild-type cells were transfected with the indicated constructs and treated with BrdU for 2 h. The cells were then fixed and examined by immunofluorescence for BrdU incorporation by examination of GFP-positive cells. The graphed data indicate that there is an increase in DNA synthesis when p27 and Spy1 are coexpressed in comparison to p27 alone. (B) The lysates from the BrdU experiment were analyzed by 10% SDS-PAGE; immunoblotting with α-flag, α-GFP, and α-p27 sera show approximately equivalent levels of protein expression.

    Article Snippet: The gels were then transferred to nitrocellulose membrane, immunoblotted with 1:2000 α-p27 (Santa Cruz Biotechnology, Santa Cruz, CA), 1:2000 α-CDK2, 1:4000 α-myc (9E10), 1:2000 α-flag (Sigma), or 1:500 α-Spy1 followed by ECL (Amersham, San Francisco, CA).

    Techniques: Transfection, Construct, Immunofluorescence, BrdU Incorporation Assay, DNA Synthesis, SDS Page, Expressing

    p27 binds to Spy1 in vivo. (A) 293T cells were transiently transfected with the indicated constructs, lysed, immunoprecipitated with α-p27 sera, analyzed by 10% SDS-PAGE, and transferred to nitrocellulose membrane. The membrane was then immunoblotted with α-myc sera to detect myc-tagged Spy1 (top panel). As shown in lane 8 of the top panel, p27 can coimmunoprecipitate with myc-tagged Spy1. The bottom panel demonstrates the approximately equal expression of exogenous p27. (B) 293T cells were transfected with mock or flag-Spy1 constructs, starved, lysed, and immunoprecipitated with α-p27 sera. Immunoblotting with α-flag sera shows that flag-Spy1 interacts with endogenous p27 (lane 4). (C) 293T cells were starved, lysed, and immunoprecipitated with α-p27 or α-Spy1 sera. Immunoblotting demonstrates that endogenous Spy1 interacts with endogenous p27 (lanes 1 and 2). A sample with no primary antibody was used as a negative control (lane 3).

    Journal: Molecular Biology of the Cell

    Article Title: Spy1 Interacts with p27Kip1 to Allow G1/S Progression

    doi: 10.1091/mbc.E02-12-0820

    Figure Lengend Snippet: p27 binds to Spy1 in vivo. (A) 293T cells were transiently transfected with the indicated constructs, lysed, immunoprecipitated with α-p27 sera, analyzed by 10% SDS-PAGE, and transferred to nitrocellulose membrane. The membrane was then immunoblotted with α-myc sera to detect myc-tagged Spy1 (top panel). As shown in lane 8 of the top panel, p27 can coimmunoprecipitate with myc-tagged Spy1. The bottom panel demonstrates the approximately equal expression of exogenous p27. (B) 293T cells were transfected with mock or flag-Spy1 constructs, starved, lysed, and immunoprecipitated with α-p27 sera. Immunoblotting with α-flag sera shows that flag-Spy1 interacts with endogenous p27 (lane 4). (C) 293T cells were starved, lysed, and immunoprecipitated with α-p27 or α-Spy1 sera. Immunoblotting demonstrates that endogenous Spy1 interacts with endogenous p27 (lanes 1 and 2). A sample with no primary antibody was used as a negative control (lane 3).

    Article Snippet: The gels were then transferred to nitrocellulose membrane, immunoblotted with 1:2000 α-p27 (Santa Cruz Biotechnology, Santa Cruz, CA), 1:2000 α-CDK2, 1:4000 α-myc (9E10), 1:2000 α-flag (Sigma), or 1:500 α-Spy1 followed by ECL (Amersham, San Francisco, CA).

    Techniques: In Vivo, Transfection, Construct, Immunoprecipitation, SDS Page, Expressing, Negative Control

    p27 interacts with Spy1 and CDK2. 293T cells were transfected with the indicated constructs. The lysates were immunoprecipitated with α-p27 or α–CDK2 sera and immunoblotted for Spy1, CDK2, and p27. Lane 8 demonstrates that flag-Spy1 (top panel), endogenous CDK2 (middle panel), and p27 (bottom panel) can coimmunoprecipitate. The top panel of lane 11 shows that Spy1 interacts with CDK2 and that this interaction is increased when p27 is overexpressed as demonstrated in lane 12.

    Journal: Molecular Biology of the Cell

    Article Title: Spy1 Interacts with p27Kip1 to Allow G1/S Progression

    doi: 10.1091/mbc.E02-12-0820

    Figure Lengend Snippet: p27 interacts with Spy1 and CDK2. 293T cells were transfected with the indicated constructs. The lysates were immunoprecipitated with α-p27 or α–CDK2 sera and immunoblotted for Spy1, CDK2, and p27. Lane 8 demonstrates that flag-Spy1 (top panel), endogenous CDK2 (middle panel), and p27 (bottom panel) can coimmunoprecipitate. The top panel of lane 11 shows that Spy1 interacts with CDK2 and that this interaction is increased when p27 is overexpressed as demonstrated in lane 12.

    Article Snippet: The gels were then transferred to nitrocellulose membrane, immunoblotted with 1:2000 α-p27 (Santa Cruz Biotechnology, Santa Cruz, CA), 1:2000 α-CDK2, 1:4000 α-myc (9E10), 1:2000 α-flag (Sigma), or 1:500 α-Spy1 followed by ECL (Amersham, San Francisco, CA).

    Techniques: Transfection, Construct, Immunoprecipitation

    JQ1 decreased MYC and elevated p21 protein abundance in human ATC cell lines. (ai) Immunohistochemical analysis for MYC protein was carried out after the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines were treated with vehicle or with JQ1 (500 nM) for 48 hours. (aii) Quantification of MYC-positive cells indicated reduction of MYC protein by JQ1. (bi–biv) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against MYC, p21, p27, cyclin D1, and CDK4 and the loading control α -tubulin, as described in the Materials and Methods section. (ci–civ) Band intensities in (b) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (di–div) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against p -Rb, total Rb, E2F-1, and E2F-3 and the loading control α -tubulin, as described in the Materials and Methods section. (ei–eiv) Band intensities in (di–div) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (fi–fiii) JQ1 inhibited cell cycle progression of ATC cell lines. (fi) Cell cycle profiles in THJ cell lines. The percentages of cell populations of different cell cycle phases are shown in the upper-right corner. After JQ1 treatments, all THJ cell lines were blocked in the G1/G0 phase, and there was reduction in the S and G2/M phases. (fii) JQ1 treatment lengthened the G1/G0 phase in ATC cells. (fiii) JQ1 treatment affected the distribution of cell cycle. Different cell cycle phases were quantified by 4′,6-diamidino-2-phenylindole staining, followed by fluorescence-activated cell sorting analysis in THJ cell lines.

    Journal: The Journal of Clinical Endocrinology and Metabolism

    Article Title: Targeting MYC as a Therapeutic Intervention for Anaplastic Thyroid Cancer

    doi: 10.1210/jc.2016-3771

    Figure Lengend Snippet: JQ1 decreased MYC and elevated p21 protein abundance in human ATC cell lines. (ai) Immunohistochemical analysis for MYC protein was carried out after the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines were treated with vehicle or with JQ1 (500 nM) for 48 hours. (aii) Quantification of MYC-positive cells indicated reduction of MYC protein by JQ1. (bi–biv) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against MYC, p21, p27, cyclin D1, and CDK4 and the loading control α -tubulin, as described in the Materials and Methods section. (ci–civ) Band intensities in (b) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (di–div) Cell lysates were prepared from the THJ-11T, THJ-16T, THJ-21T, and THJ-29T cell lines. The blots were probed with the antibodies against p -Rb, total Rb, E2F-1, and E2F-3 and the loading control α -tubulin, as described in the Materials and Methods section. (ei–eiv) Band intensities in (di–div) were quantified, allowing a comparison between vehicle-treated and JQ1-treated cells. The P values are shown. (fi–fiii) JQ1 inhibited cell cycle progression of ATC cell lines. (fi) Cell cycle profiles in THJ cell lines. The percentages of cell populations of different cell cycle phases are shown in the upper-right corner. After JQ1 treatments, all THJ cell lines were blocked in the G1/G0 phase, and there was reduction in the S and G2/M phases. (fii) JQ1 treatment lengthened the G1/G0 phase in ATC cells. (fiii) JQ1 treatment affected the distribution of cell cycle. Different cell cycle phases were quantified by 4′,6-diamidino-2-phenylindole staining, followed by fluorescence-activated cell sorting analysis in THJ cell lines.

    Article Snippet: The antibodies against MYC were used (1:5000 dilution; ab32072); cyclin-dependent kinase 4 (CDK4) (1:2500 dilution; ab75511) from Abcam; p21 (1:200 dilution; sc-6246), E2F-1 (1:200 dilution; sc-251), E2F-3 (1:200 dilution; sc-878), and TWIST1 (1:200 dilution; sc-81417) from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA); phosphorylated Rb (S780) (1:1000 dilution; #9307), Rb (1:2000 dilution; #9309), p27 (1:1000 dilution; #3686), zinc finger protein SNAIL (Snail; 1:1000 dilution; #3895), and Slug (1:1000 dilution; #9585) from Cell Signaling; α -tubulin (1:5000 dilution; T6199) from Sigma-Aldrich; cyclin D1 (1:2000 dilution; RB9041) from Thermo Fisher Scientific (Fremont, CA); and hexamethylene bis-acetamide inducible 1 (HEXIM1; 1:2000 dilution; A303-113A) and BRD4 (1:5000 dilution; A301-985A) from Bethyl Laboratories, Inc. After being washed, the membranes were incubated with horseradish peroxidase-conjugated anti-mouse immunoglobulin G (IgG) (1:2500 dilution; NA9310 GE Healthcare) or anti-rabbit IgG (1:2500 dilution; NA9340 GE Healthcare) as the secondary antibody and were subsequently detected by means of an ECL system (Western Lightning® Plus-ECL, PerkinElmer, Waltham, MA).

    Techniques: Immunohistochemistry, Staining, Fluorescence, FACS

    PCBP1 up-regulates p27 expression by enhancing the mRNA stability and translation. ( a ) Immunoblot of endogenous p27 protein levels upon transcription inhibition or/and proteasome degradation repression. A2780 cells overexpressing GFP-PCBP1 or GFP alone were treated with DMSO, Act D at 0.5 μg/ml for 8 h, MG132 at 20 μM for 4 h, or with their combination for 4 h, and analyzed. Results are representative of at least three independent experiments. ( b ) Immunoblot of endogenous p27 protein levels in A2780 cells with endogenous PCBP1 knockdown. Cells were treated with MG132 as in ( a ) ( c ) Immunoblot of p27 ubiquitin ligase Skp2 and p27 expression in the indicated cells. No evident Skp2 expression alteration is shown. ( d ) Immunoblot of the indicated proteins possibly related to p27 protein expression and cell survival. ( e ) Semi-quantitative RT-PCR analysis of p27 or c-myc mRNA stability in A2780 cells overexpressing PCBP1 or GFP control, on condition of Act D treatment to terminate the novel mRNA transcription. c-myc and GAPDH were used as positive and negative controls. The PCR of p27 were performed with 20 cycles, c-Myc with 25 and GAPDH for 20 cycles, respectively. Relative p27 and c-myc level against GAPDH were further normalized against DMSO treated GFP and shown at the bottom. ( f ) Semi-quantitative RT-PCR analyses of p27 or c-myc mRNA stability in A2780 cells with endogenous PCBP1 knockdown by specific shRNAs as the method in E. * p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: PCBP1 up-regulates p27 expression by enhancing the mRNA stability and translation. ( a ) Immunoblot of endogenous p27 protein levels upon transcription inhibition or/and proteasome degradation repression. A2780 cells overexpressing GFP-PCBP1 or GFP alone were treated with DMSO, Act D at 0.5 μg/ml for 8 h, MG132 at 20 μM for 4 h, or with their combination for 4 h, and analyzed. Results are representative of at least three independent experiments. ( b ) Immunoblot of endogenous p27 protein levels in A2780 cells with endogenous PCBP1 knockdown. Cells were treated with MG132 as in ( a ) ( c ) Immunoblot of p27 ubiquitin ligase Skp2 and p27 expression in the indicated cells. No evident Skp2 expression alteration is shown. ( d ) Immunoblot of the indicated proteins possibly related to p27 protein expression and cell survival. ( e ) Semi-quantitative RT-PCR analysis of p27 or c-myc mRNA stability in A2780 cells overexpressing PCBP1 or GFP control, on condition of Act D treatment to terminate the novel mRNA transcription. c-myc and GAPDH were used as positive and negative controls. The PCR of p27 were performed with 20 cycles, c-Myc with 25 and GAPDH for 20 cycles, respectively. Relative p27 and c-myc level against GAPDH were further normalized against DMSO treated GFP and shown at the bottom. ( f ) Semi-quantitative RT-PCR analyses of p27 or c-myc mRNA stability in A2780 cells with endogenous PCBP1 knockdown by specific shRNAs as the method in E. * p

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Expressing, Inhibition, Activated Clotting Time Assay, Quantitative RT-PCR, Polymerase Chain Reaction

    Relevance of PCBP1 to p27 expression in human cancer samples. ( a ) Representative IHC staining of PCBP1 and p27 protein expression in tumor adjacent normal and tumor regions of ovary carcinoma. Scale bars are equal to 50 μm. ( b ) Statistical analysis of PCBP1 and p27 in normal and malignant tissues of ovary. 18 normal tissues and 21 carcinoma tissues were analyzed. The unpaired student t test was used to check the group difference. p values are shown. ( c ) Representative IHC staining of PCBP1 and p27 protein expression in the paired adjacent normal and tumor regions of colon carcinoma. Scale bars are equal to 50 μm. ( d ) Statistical analysis of PCBP1 and p27 expression in 10 paired fresh normal and malignant tissues of colon tissues. The paired student t test was carried out to check the group difference. p values are shown. ( e ) Representative IHC staining of p27 ubiquitin ligase, Skp2 protein expression in tumor adjacent normal and tumor regions of colon carcinoma. No evident Skp2 expression difference was observed. Scale bars are equal to 50 μm

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: Relevance of PCBP1 to p27 expression in human cancer samples. ( a ) Representative IHC staining of PCBP1 and p27 protein expression in tumor adjacent normal and tumor regions of ovary carcinoma. Scale bars are equal to 50 μm. ( b ) Statistical analysis of PCBP1 and p27 in normal and malignant tissues of ovary. 18 normal tissues and 21 carcinoma tissues were analyzed. The unpaired student t test was used to check the group difference. p values are shown. ( c ) Representative IHC staining of PCBP1 and p27 protein expression in the paired adjacent normal and tumor regions of colon carcinoma. Scale bars are equal to 50 μm. ( d ) Statistical analysis of PCBP1 and p27 expression in 10 paired fresh normal and malignant tissues of colon tissues. The paired student t test was carried out to check the group difference. p values are shown. ( e ) Representative IHC staining of p27 ubiquitin ligase, Skp2 protein expression in tumor adjacent normal and tumor regions of colon carcinoma. No evident Skp2 expression difference was observed. Scale bars are equal to 50 μm

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Expressing, Immunohistochemistry, Staining

    Proposed model of PCBP1 stabilizing p27 mRNA to repress cell transformation and carcinogenesis. PCBP1 binds to p27 mRNA 3'-UTR region via 5'-AUUAAGUAAU-3' to stabilize mRNA against degradation, while enhance the translation, resulting in more p27 protein that participates in cell cycle surveillance to maintain cell homeostasis and to inhibit carcinogenesis, while p27 degradation by ubiquitin ligase Skp2 promotes cell cycle progression after the proper surveillance. In tumor tissues, anti-cancer drugs can induce p27 expression to induce tumor cell cycle arrest and apoptosis. Loss of PCBP1 expression would expose p27 mRNA for degradation, leading to lower expression of p27 protein and unregulated cell proliferation, eventually hyperplasia and carcinogenesis, which are independent of Skp2 status

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: Proposed model of PCBP1 stabilizing p27 mRNA to repress cell transformation and carcinogenesis. PCBP1 binds to p27 mRNA 3'-UTR region via 5'-AUUAAGUAAU-3' to stabilize mRNA against degradation, while enhance the translation, resulting in more p27 protein that participates in cell cycle surveillance to maintain cell homeostasis and to inhibit carcinogenesis, while p27 degradation by ubiquitin ligase Skp2 promotes cell cycle progression after the proper surveillance. In tumor tissues, anti-cancer drugs can induce p27 expression to induce tumor cell cycle arrest and apoptosis. Loss of PCBP1 expression would expose p27 mRNA for degradation, leading to lower expression of p27 protein and unregulated cell proliferation, eventually hyperplasia and carcinogenesis, which are independent of Skp2 status

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Transformation Assay, Expressing

    PCBP1 binds to p27 transcript to increase its expression. ( a ) Identification of the purely PCBP1-bound mRNAs by RNA sequencing. mRNA numbers are indicated as copy number. ( b ) RT-PCR validation of PCBP1-associated p27 mRNA from the precipitated mRNA pools in A. p21 and GAPDH transcripts are respectively used as the positive and negative controls of PCBP1-bound mRNA. ( c ) RT-PCR detection of endogenous p27 mRNA immunoprecipitated by PCBP1-specific antibody. Normal IgG is used as negative control for RIP. c-Myc and GAPDH are used as positive or negative control of PCBP1-bound mRNA, respectively. ( d ) Quantitative RT-PCR detection of p27 mRNA in A2780 cells with overexpressing or silencing endogenous PCBP1. Three independent experiments were carried out and analyzed. Data are shown as means±SD. * p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: PCBP1 binds to p27 transcript to increase its expression. ( a ) Identification of the purely PCBP1-bound mRNAs by RNA sequencing. mRNA numbers are indicated as copy number. ( b ) RT-PCR validation of PCBP1-associated p27 mRNA from the precipitated mRNA pools in A. p21 and GAPDH transcripts are respectively used as the positive and negative controls of PCBP1-bound mRNA. ( c ) RT-PCR detection of endogenous p27 mRNA immunoprecipitated by PCBP1-specific antibody. Normal IgG is used as negative control for RIP. c-Myc and GAPDH are used as positive or negative control of PCBP1-bound mRNA, respectively. ( d ) Quantitative RT-PCR detection of p27 mRNA in A2780 cells with overexpressing or silencing endogenous PCBP1. Three independent experiments were carried out and analyzed. Data are shown as means±SD. * p

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Expressing, RNA Sequencing Assay, Reverse Transcription Polymerase Chain Reaction, Immunoprecipitation, Negative Control, Quantitative RT-PCR

    PCBP1 suppresses cell proliferation and tumorigenesis. ( a , b ) Cell viability analyses of A2780 ( a ) and DLD-1 ( b ) cells stably expressing PCBP1, PCBP1-p27 KD, p27 KD or GFP control by MTT assays. Data are presented as mean±SD (** P

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: PCBP1 suppresses cell proliferation and tumorigenesis. ( a , b ) Cell viability analyses of A2780 ( a ) and DLD-1 ( b ) cells stably expressing PCBP1, PCBP1-p27 KD, p27 KD or GFP control by MTT assays. Data are presented as mean±SD (** P

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Stable Transfection, Expressing, MTT Assay

    Overexpression of PCBP1 represses cell cycle progression and promotes apoptosis. ( a ) Flow cytometry analysis of cell cycle progression in A2780 and DLD-1 cells stably transfected with PCBP1 or PCBP1 with additional p27 knockdown. ( b ) The effect of PCBP1 and p27 in cell cycle progression of DLD-1 and A2780 cells. The populations of cells in G1, S and G2 phases are presented based on three independent experiments. * P

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: PCBP1 depletion promotes tumorigenesis through attenuation of p27Kip1 mRNA stability and translation

    doi: 10.1186/s13046-018-0840-1

    Figure Lengend Snippet: Overexpression of PCBP1 represses cell cycle progression and promotes apoptosis. ( a ) Flow cytometry analysis of cell cycle progression in A2780 and DLD-1 cells stably transfected with PCBP1 or PCBP1 with additional p27 knockdown. ( b ) The effect of PCBP1 and p27 in cell cycle progression of DLD-1 and A2780 cells. The populations of cells in G1, S and G2 phases are presented based on three independent experiments. * P

    Article Snippet: Tissues were formalin-fixed, paraffin-embedded and sliced into 6 μm thin sections using Leica BM 2135 microtome, which were subsequently stained with anti-PCBP1 (1:200 dilution, Abcam), anti-p27 (1:200 dilution, ExCell Bio) and Skp2 (1:200 dilution, CST) antibodies.

    Techniques: Over Expression, Flow Cytometry, Cytometry, Stable Transfection, Transfection

    EL regulates the expression of G 1 -phase related genes. A549, H441, and H520 cells were treated with EL (100 μM) for 24 h. Relative mRNA expression levels for cyclin D1 , CDK2 , CDK4 , cdc25A , p21 WAF1/CIP1 , and p27 KIP1 were determined by quantitative

    Journal: Nutrition and cancer

    Article Title: Enterolactone induces G1-phase cell cycle arrest in non-small cell lung cancer cells by down-regulating cyclins and cyclin-dependent kinases

    doi: 10.1080/01635581.2017.1296169

    Figure Lengend Snippet: EL regulates the expression of G 1 -phase related genes. A549, H441, and H520 cells were treated with EL (100 μM) for 24 h. Relative mRNA expression levels for cyclin D1 , CDK2 , CDK4 , cdc25A , p21 WAF1/CIP1 , and p27 KIP1 were determined by quantitative

    Article Snippet: Antibodies for cyclin D1, p-pRb, CDK2, CDK4, CDK6, p21/Cip1, p27/Kip1, t-cdc25A, and GAPDH were purchased from Cell Signaling Technology (Danvers, MA).

    Techniques: Expressing

    E2F EMSAs. (A) The positions, directions, and sequences of the putative E2F sites of the rat, mouse, and human p27KIP1 promoters are depicted. The sequences of consensus E2F and E2F4-DP1 sites are indicated. The forward consensus sites are indicated by underlining, and the reverse consensus sites are indicated by bold and italics. Base pair numbers are relative to the translation start site for the p27 protein. (B) EMSAs using control (Babe) and LMP1 nuclear lysates were performed. Complexes were competed with a 200-fold excess of consensus (comp) and mutant oligonucleotides. Supershifts with the indicated antibodies were performed. The arrow indicates the position of nonspecific complexes, and boxes highlight the positions of specific complexes. Arrowheads indicate the positions of the antibody-shifted complexes for E2F4 (closed arrowhead) and p130 (open arrowhead). Lane numbers are indicated below.

    Journal: Journal of Virology

    Article Title: Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation ▿

    doi: 10.1128/JVI.01422-09

    Figure Lengend Snippet: E2F EMSAs. (A) The positions, directions, and sequences of the putative E2F sites of the rat, mouse, and human p27KIP1 promoters are depicted. The sequences of consensus E2F and E2F4-DP1 sites are indicated. The forward consensus sites are indicated by underlining, and the reverse consensus sites are indicated by bold and italics. Base pair numbers are relative to the translation start site for the p27 protein. (B) EMSAs using control (Babe) and LMP1 nuclear lysates were performed. Complexes were competed with a 200-fold excess of consensus (comp) and mutant oligonucleotides. Supershifts with the indicated antibodies were performed. The arrow indicates the position of nonspecific complexes, and boxes highlight the positions of specific complexes. Arrowheads indicate the positions of the antibody-shifted complexes for E2F4 (closed arrowhead) and p130 (open arrowhead). Lane numbers are indicated below.

    Article Snippet: Primary antibodies included actin and hemagglutinin (HA) tag (Cell Signaling), LMP1-specific antibodies (Cao 7E10, Cao 8G3, LMP1 IG6, and Cao 7G8; Ascenion GmbH), p27 (Santa Cruz), and myc tag (Upstate).

    Techniques: Mutagenesis

    Regulation of ectopic p27. The ability of LMP1 to posttranscriptionally regulate ectopically expressed p27 was determined. Control and LMP1 stable cell lines were transfected with myc-tagged p27 and selected for 48 h with G418. Cell lysates from control (Babe) or LMP1 stable cells transfected with vector (DNA3) or p27-expressing plasmids were analyzed by Western blotting for p27 and LMP1 expression. A 7.5-μg amount of protein was loaded per lane. The positions of myc-tagged and endogenous p27 proteins are indicated by the arrows. The positions of the molecular weight markers (in thousands) are indicated by the closed arrowheads.

    Journal: Journal of Virology

    Article Title: Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation ▿

    doi: 10.1128/JVI.01422-09

    Figure Lengend Snippet: Regulation of ectopic p27. The ability of LMP1 to posttranscriptionally regulate ectopically expressed p27 was determined. Control and LMP1 stable cell lines were transfected with myc-tagged p27 and selected for 48 h with G418. Cell lysates from control (Babe) or LMP1 stable cells transfected with vector (DNA3) or p27-expressing plasmids were analyzed by Western blotting for p27 and LMP1 expression. A 7.5-μg amount of protein was loaded per lane. The positions of myc-tagged and endogenous p27 proteins are indicated by the arrows. The positions of the molecular weight markers (in thousands) are indicated by the closed arrowheads.

    Article Snippet: Primary antibodies included actin and hemagglutinin (HA) tag (Cell Signaling), LMP1-specific antibodies (Cao 7E10, Cao 8G3, LMP1 IG6, and Cao 7G8; Ascenion GmbH), p27 (Santa Cruz), and myc tag (Upstate).

    Techniques: Stable Transfection, Transfection, Plasmid Preparation, Expressing, Western Blot, Molecular Weight

    Downregulation of p27 protein by LMP1 and LMP1 mutants. Control (Babe) and wild-type and mutant LMP1 stable Rat-1 cells were assayed by Western blotting for p27 compared to actin (loading control). Expression of tagged LMP1 constructs was confirmed with HA antibodies. p27 expression was quantitated relative to actin levels using the Li-Cor Odyssey imaging system and indicated as a value relative to Babe cells set as 100. The positions of the molecular weight markers (in thousands) are indicated by the closed arrowheads.

    Journal: Journal of Virology

    Article Title: Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation ▿

    doi: 10.1128/JVI.01422-09

    Figure Lengend Snippet: Downregulation of p27 protein by LMP1 and LMP1 mutants. Control (Babe) and wild-type and mutant LMP1 stable Rat-1 cells were assayed by Western blotting for p27 compared to actin (loading control). Expression of tagged LMP1 constructs was confirmed with HA antibodies. p27 expression was quantitated relative to actin levels using the Li-Cor Odyssey imaging system and indicated as a value relative to Babe cells set as 100. The positions of the molecular weight markers (in thousands) are indicated by the closed arrowheads.

    Article Snippet: Primary antibodies included actin and hemagglutinin (HA) tag (Cell Signaling), LMP1-specific antibodies (Cao 7E10, Cao 8G3, LMP1 IG6, and Cao 7G8; Ascenion GmbH), p27 (Santa Cruz), and myc tag (Upstate).

    Techniques: Mutagenesis, Western Blot, Expressing, Construct, Imaging, Molecular Weight

    Regulation of p27 RNA by LMP1 mutants. RPAs were performed using total RNA from stable cell lines. Fragments protected by rat p27KIP1 RNA probe relative to control (GAPDH) RNA probe were quantitated using a PhosphorImager, and p27 expression is depicted relative to that in control (Babe) stable cells, which was set arbitrarily as 100. Means of three independent experiments are presented with error bars representing the standard deviations.

    Journal: Journal of Virology

    Article Title: Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation ▿

    doi: 10.1128/JVI.01422-09

    Figure Lengend Snippet: Regulation of p27 RNA by LMP1 mutants. RPAs were performed using total RNA from stable cell lines. Fragments protected by rat p27KIP1 RNA probe relative to control (GAPDH) RNA probe were quantitated using a PhosphorImager, and p27 expression is depicted relative to that in control (Babe) stable cells, which was set arbitrarily as 100. Means of three independent experiments are presented with error bars representing the standard deviations.

    Article Snippet: Primary antibodies included actin and hemagglutinin (HA) tag (Cell Signaling), LMP1-specific antibodies (Cao 7E10, Cao 8G3, LMP1 IG6, and Cao 7G8; Ascenion GmbH), p27 (Santa Cruz), and myc tag (Upstate).

    Techniques: Stable Transfection, Expressing

    Regulation of the p27KIP promoter by LMP1 mutants. Promoter reporter assays were performed by transfection of 293T cells with control pRL-SV40 with pGL3-Basic (empty reporter) or p27 (p27-1501 and p27-554) reporter plasmids and vector control (Babe) or plasmids expressing LMP1 (A). p27 promoter plasmids contain 1,500 and 554 bp of the Rattus no r vegicus p27KIP1 promoter relative to the translation start site. Forty hours posttransfection, cells were harvested and dual-luciferase assays were performed. Relative luciferase activity was determined by the firefly luciferase activity of the reporter constructs relative to the control R enilla luciferase activity. Each condition was used in triplicate, and the means of three independent experiments are presented. Error bars represent the standard deviations from the independent experiments. In parallel, cells were harvested for Western blotting (B). Levels of wild-type LMP1 and LMP1 mutants were determined by blotting for LMP1 and HA tag. Actin blotting confirmed equal loading. The positions of the molecular weight markers (in thousands) are indicated.

    Journal: Journal of Virology

    Article Title: Transcriptional Downregulation of p27KIP1 through Regulation of E2F Function during LMP1-Mediated Transformation ▿

    doi: 10.1128/JVI.01422-09

    Figure Lengend Snippet: Regulation of the p27KIP promoter by LMP1 mutants. Promoter reporter assays were performed by transfection of 293T cells with control pRL-SV40 with pGL3-Basic (empty reporter) or p27 (p27-1501 and p27-554) reporter plasmids and vector control (Babe) or plasmids expressing LMP1 (A). p27 promoter plasmids contain 1,500 and 554 bp of the Rattus no r vegicus p27KIP1 promoter relative to the translation start site. Forty hours posttransfection, cells were harvested and dual-luciferase assays were performed. Relative luciferase activity was determined by the firefly luciferase activity of the reporter constructs relative to the control R enilla luciferase activity. Each condition was used in triplicate, and the means of three independent experiments are presented. Error bars represent the standard deviations from the independent experiments. In parallel, cells were harvested for Western blotting (B). Levels of wild-type LMP1 and LMP1 mutants were determined by blotting for LMP1 and HA tag. Actin blotting confirmed equal loading. The positions of the molecular weight markers (in thousands) are indicated.

    Article Snippet: Primary antibodies included actin and hemagglutinin (HA) tag (Cell Signaling), LMP1-specific antibodies (Cao 7E10, Cao 8G3, LMP1 IG6, and Cao 7G8; Ascenion GmbH), p27 (Santa Cruz), and myc tag (Upstate).

    Techniques: Transfection, Plasmid Preparation, Expressing, Luciferase, Activity Assay, Construct, Western Blot, Molecular Weight

    Mitochondrial p27 is sufficient to induce endothelial cell migration. (A, B) Endothelial cells were treated with 50 μM caffeine for 18 hours, and mitochondrial (“mito”) and nonmitochondrial (“non-mito”) fractions were separated. p27 and the closely related p21 protein were detected by immunoblot; TIM23 and Trx-1 served as purity controls for the fractions. (A) Representative immunoblots. (B) Semiquantitative analysis of mitochondrial p27 normalized to TIM23. Data are mean ± SEM, n = 6, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Mitochondrial p27 is sufficient to induce endothelial cell migration. (A, B) Endothelial cells were treated with 50 μM caffeine for 18 hours, and mitochondrial (“mito”) and nonmitochondrial (“non-mito”) fractions were separated. p27 and the closely related p21 protein were detected by immunoblot; TIM23 and Trx-1 served as purity controls for the fractions. (A) Representative immunoblots. (B) Semiquantitative analysis of mitochondrial p27 normalized to TIM23. Data are mean ± SEM, n = 6, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Migration, Western Blot

    The N- and C-terminus of p27 are required for endothelial cell migration and ATP content. (A) Schematic representation of mitochondrially targeted p27 deletion mutants lacking the N-terminus (“ΔN”), the C-terminus (“ΔC”), or both (“ΔNΔC”). The full-length protein (“fl”) and all mutants contain an N-terminal mitochondrial targeting sequence (“MTS,” red) and a C-terminal myc tag (green). Numbers indicate the deletion endpoints within p27. (B-E) Endothelial cells were transfected with an empty vector (“EV”) or expression vectors for the mitochondrially targeted p27 mutants depicted in (A). (B, C) Expression and localization of the mitochondrially targeted mutant p27 proteins were analyzed by immunoblot and immunofluorescence. (B) Representative immunoblot, tubulin served as loading control. (C) Representative immunostainings: nuclei were visualized with DAPI (blue), mitochondria by staining for TIM23 (red), and the targeted p27 mutants by staining for the myc epitope (“myc (p27),” green). Merge shows an overlay of all fluorescence channels. (D) Migratory capacity was measured in a scratch wound assay by counting cells migrated into the wound using Image J. Data are mean ± SEM, n = 6, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: The N- and C-terminus of p27 are required for endothelial cell migration and ATP content. (A) Schematic representation of mitochondrially targeted p27 deletion mutants lacking the N-terminus (“ΔN”), the C-terminus (“ΔC”), or both (“ΔNΔC”). The full-length protein (“fl”) and all mutants contain an N-terminal mitochondrial targeting sequence (“MTS,” red) and a C-terminal myc tag (green). Numbers indicate the deletion endpoints within p27. (B-E) Endothelial cells were transfected with an empty vector (“EV”) or expression vectors for the mitochondrially targeted p27 mutants depicted in (A). (B, C) Expression and localization of the mitochondrially targeted mutant p27 proteins were analyzed by immunoblot and immunofluorescence. (B) Representative immunoblot, tubulin served as loading control. (C) Representative immunostainings: nuclei were visualized with DAPI (blue), mitochondria by staining for TIM23 (red), and the targeted p27 mutants by staining for the myc epitope (“myc (p27),” green). Merge shows an overlay of all fluorescence channels. (D) Migratory capacity was measured in a scratch wound assay by counting cells migrated into the wound using Image J. Data are mean ± SEM, n = 6, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Migration, Sequencing, Transfection, Plasmid Preparation, Expressing, Mutagenesis, Immunofluorescence, Staining, Fluorescence, Scratch Wound Assay Assay

    Caffeine effects in the heart depend on p27. (A) The mouse cardiomyocyte cell line HL-1 was lentivirally transduced with an empty vector (“EV”) or an expression vector for mitochondrially targeted p27 (“mito p27”) and treated with 500 μM H 2 O 2 for 48 hours. Apoptosis was measured as annexin V positive/7-PI negative cells by flow cytometry. Data are mean ± SEM, n = 5, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Caffeine effects in the heart depend on p27. (A) The mouse cardiomyocyte cell line HL-1 was lentivirally transduced with an empty vector (“EV”) or an expression vector for mitochondrially targeted p27 (“mito p27”) and treated with 500 μM H 2 O 2 for 48 hours. Apoptosis was measured as annexin V positive/7-PI negative cells by flow cytometry. Data are mean ± SEM, n = 5, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Transduction, Plasmid Preparation, Expressing, Flow Cytometry, Cytometry

    p27 is required for endothelial cell migration. (A, B) p27 was knocked down in endothelial cells by transfection with 2 different siRNAs targeting the p27 mRNA (“p27 siRNA-1,” “p27 siRNA-2”) or a scrambled siRNA (“scr”) as control, and p27 levels were determined by immunoblot. (A) Representative immunoblots, Actin served as loading control. (B) Knockdown efficiency was determined by semiquantitative analysis of immunoblots. Data are mean ± SEM, n = 5, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: p27 is required for endothelial cell migration. (A, B) p27 was knocked down in endothelial cells by transfection with 2 different siRNAs targeting the p27 mRNA (“p27 siRNA-1,” “p27 siRNA-2”) or a scrambled siRNA (“scr”) as control, and p27 levels were determined by immunoblot. (A) Representative immunoblots, Actin served as loading control. (B) Knockdown efficiency was determined by semiquantitative analysis of immunoblots. Data are mean ± SEM, n = 5, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Migration, Transfection, Western Blot

    Serine 10 and threonine 187 of p27 are required for endothelial cell migration and mitochondrial import. (A, B) Endothelial cells were treated with caffeine for 18 hours or left untreated, and phosphorylation of serine 10 (“p27 P-S10”) and threonine 187 (“p27 P-T187), as well as total p27 (“p27”), were detected by immunoblot. (A) Representative immunoblots with the corresponding loading control (Tubulin) below the respective immunoblot. The asterisk denotes p27 phosphorylated on threonine 187. (B) Semiquantitative analyses of the ratio of phosphorylated p27 to total p27 for both phosphorylation events. Data are mean ± SEM, n = 7: p27 P-S10, n = 6: p27 P-T187, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Serine 10 and threonine 187 of p27 are required for endothelial cell migration and mitochondrial import. (A, B) Endothelial cells were treated with caffeine for 18 hours or left untreated, and phosphorylation of serine 10 (“p27 P-S10”) and threonine 187 (“p27 P-T187), as well as total p27 (“p27”), were detected by immunoblot. (A) Representative immunoblots with the corresponding loading control (Tubulin) below the respective immunoblot. The asterisk denotes p27 phosphorylated on threonine 187. (B) Semiquantitative analyses of the ratio of phosphorylated p27 to total p27 for both phosphorylation events. Data are mean ± SEM, n = 7: p27 P-S10, n = 6: p27 P-T187, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Migration, Western Blot

    Mitochondrial p27 restores the impaired αSMA up-regulation in p27-deficient cardiac fibroblasts. Fibroblasts isolated from the hearts of p27-deficient mice were lentivirally transduced with an expression vector for mitochondrially targeted p27 (“mito p27”) or a corresponding empty vector (“EV”). (A) Representative immunostainings: nuclei were visualized with DAPI (blue), mitochondria by staining for TIM23 (red), and the mitochondrially targeted p27 by staining for the myc epitope (“myc (p27),” green). Merge shows an overlay of all fluorescence channels. (B, C) Myofibroblast differentiation was induced by treatment with 2 ng/ml TGFβ1 for 48 hours, and αSMA was detected by immunoblot. (B) Representative immunoblots, Vimentin served as loading control. (C) Semiquantitative analysis of αSMA normalized to Vimentin. Data are mean ± SEM, n = 5, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Mitochondrial p27 restores the impaired αSMA up-regulation in p27-deficient cardiac fibroblasts. Fibroblasts isolated from the hearts of p27-deficient mice were lentivirally transduced with an expression vector for mitochondrially targeted p27 (“mito p27”) or a corresponding empty vector (“EV”). (A) Representative immunostainings: nuclei were visualized with DAPI (blue), mitochondria by staining for TIM23 (red), and the mitochondrially targeted p27 by staining for the myc epitope (“myc (p27),” green). Merge shows an overlay of all fluorescence channels. (B, C) Myofibroblast differentiation was induced by treatment with 2 ng/ml TGFβ1 for 48 hours, and αSMA was detected by immunoblot. (B) Representative immunoblots, Vimentin served as loading control. (C) Semiquantitative analysis of αSMA normalized to Vimentin. Data are mean ± SEM, n = 5, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Isolation, Mouse Assay, Transduction, Expressing, Plasmid Preparation, Staining, Fluorescence, Western Blot

    p27 is required for myofibroblast differentiation of cardiac fibroblasts. Cardiac fibroblasts were isolated from hearts of wild-type (“wt”) mice and p27-deficient (“p27 −/−”) littermates. Myofibroblast differentiation was induced by treatment with 2 ng/ml TGFβ1 for 48 hours in the presence or absence of 50 μM caffeine. Induction of αSMA was detected by immunoblot and immunostaining. (A) Representative immunoblots, Vimentin served as loading control. (B) Semiquantitative analysis of αSMA normalized to Vimentin. Data are mean ± SEM, n = 8: wt untreated, wt +TGFβ1, p27 −/− untreated, p27 −/− +TGFβ1; n = 5: all others, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: p27 is required for myofibroblast differentiation of cardiac fibroblasts. Cardiac fibroblasts were isolated from hearts of wild-type (“wt”) mice and p27-deficient (“p27 −/−”) littermates. Myofibroblast differentiation was induced by treatment with 2 ng/ml TGFβ1 for 48 hours in the presence or absence of 50 μM caffeine. Induction of αSMA was detected by immunoblot and immunostaining. (A) Representative immunoblots, Vimentin served as loading control. (B) Semiquantitative analysis of αSMA normalized to Vimentin. Data are mean ± SEM, n = 8: wt untreated, wt +TGFβ1, p27 −/− untreated, p27 −/− +TGFβ1; n = 5: all others, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Isolation, Mouse Assay, Immunostaining, Western Blot

    Caffeine enhances respiration, ATP content, and mitochondrial localization of p27 in old mouse hearts. (A-D) Twenty-two-month-old wild-type mice received drinking water (“old”) or water supplemented with 0.05% caffeine for 10 days (“old+caffeine”). (A) O 2 consumption was measured in isolated heart mitochondria without the addition of substrates (“mito”) and after the successive addition of malate/glutamate (“M/G”), ADP, rotenone (“rot”), and succinate (“succ”) (left panel). The right panel shows a magnification of O 2 consumption after the addition of malate/glutamate and ADP, respectively. Data are mean ± SEM, n = 6 per group, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Caffeine enhances respiration, ATP content, and mitochondrial localization of p27 in old mouse hearts. (A-D) Twenty-two-month-old wild-type mice received drinking water (“old”) or water supplemented with 0.05% caffeine for 10 days (“old+caffeine”). (A) O 2 consumption was measured in isolated heart mitochondria without the addition of substrates (“mito”) and after the successive addition of malate/glutamate (“M/G”), ADP, rotenone (“rot”), and succinate (“succ”) (left panel). The right panel shows a magnification of O 2 consumption after the addition of malate/glutamate and ADP, respectively. Data are mean ± SEM, n = 6 per group, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Mouse Assay, Isolation

    Caffeine improves outcomes after myocardial infarction in prediabetic mice and induces mitochondrial translocation of p27. Two-month-old wild-type mice were fed a diabetogenic diet for 11 weeks. For the last 10 days, one group of animals received drinking water supplemented with 0.05% caffeine. Afterward, myocardial infarction was induced by ligation of the left anterior descending coronary artery for 60 minutes followed by reperfusion. Twenty-one days after infarction, hearts were excised, sectioned, and the sections stained. (A) Representative Gomori stainings of sections of 3 different hearts for each dietary regimen. (B) Infarct size per left ventricle and (C) minimum left ventricular (“LV”) wall thickness in the infarcted myocardium. Data are mean ± SEM, n = 8: diabetogenic diet, n = 10: diabetogenic diet +caffeine, * p

    Journal: PLoS Biology

    Article Title: CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine

    doi: 10.1371/journal.pbio.2004408

    Figure Lengend Snippet: Caffeine improves outcomes after myocardial infarction in prediabetic mice and induces mitochondrial translocation of p27. Two-month-old wild-type mice were fed a diabetogenic diet for 11 weeks. For the last 10 days, one group of animals received drinking water supplemented with 0.05% caffeine. Afterward, myocardial infarction was induced by ligation of the left anterior descending coronary artery for 60 minutes followed by reperfusion. Twenty-one days after infarction, hearts were excised, sectioned, and the sections stained. (A) Representative Gomori stainings of sections of 3 different hearts for each dietary regimen. (B) Infarct size per left ventricle and (C) minimum left ventricular (“LV”) wall thickness in the infarcted myocardium. Data are mean ± SEM, n = 8: diabetogenic diet, n = 10: diabetogenic diet +caffeine, * p

    Article Snippet: Immunostaining of heart slices The sections were stained with antibodies against p27 (polyclonal, PA5-27188, Thermo Fisher Scientific, 1:25) and TIM23 (clone 32, BD Biosciences, 1:100).

    Techniques: Mouse Assay, Translocation Assay, Ligation, Staining

    Cyclin‐dependent kinases and cyclins are involved in solute carrier family 35 member F2 ( SLC 35F2) ‐ regulated cell cycle progression. A, Effects of SLC 35F2 knockout on cell cycle by FACS . B, Cell cycle distribution showed that inhibition of SLC 35F2 induced cell cycle arrest at G1 phase. C, Flow cytometry analysis of the cell cycle of SLC 35F2 overexpression and empty vector control cells. D, Ectopic expression of SLC 35F2 promoted G1/S phase transition and increased S‐phase proportion. E, F, Protein levels of CDK 2, CDK 4, CDK 6, Cyclin D1, Cyclin D3, p27 Kip1, p21 Waf1/Cip 1 and p18 INK 4C were detected by western blotting in indicated PTC cells. G, Relative mRNA expression levels of some cell cycle related genes analyzed by qPCR in SLC 35F2‐ KO group compared to control KTC ‐1 cells. Data were plotted relative to expression levels in control cells (* P

    Journal: Cancer Science

    Article Title: Solute carrier family 35 member F2 is indispensable for papillary thyroid carcinoma progression through activation of transforming growth factor‐β type I receptor/apoptosis signal‐regulating kinase 1/mitogen‐activated protein kinase signaling axis, et al. Solute carrier family 35 member F2 is indispensable for papillary thyroid carcinoma progression through activation of transforming growth factor‐β type I receptor/apoptosis signal‐regulating kinase 1/mitogen‐activated protein kinase signaling axis

    doi: 10.1111/cas.13478

    Figure Lengend Snippet: Cyclin‐dependent kinases and cyclins are involved in solute carrier family 35 member F2 ( SLC 35F2) ‐ regulated cell cycle progression. A, Effects of SLC 35F2 knockout on cell cycle by FACS . B, Cell cycle distribution showed that inhibition of SLC 35F2 induced cell cycle arrest at G1 phase. C, Flow cytometry analysis of the cell cycle of SLC 35F2 overexpression and empty vector control cells. D, Ectopic expression of SLC 35F2 promoted G1/S phase transition and increased S‐phase proportion. E, F, Protein levels of CDK 2, CDK 4, CDK 6, Cyclin D1, Cyclin D3, p27 Kip1, p21 Waf1/Cip 1 and p18 INK 4C were detected by western blotting in indicated PTC cells. G, Relative mRNA expression levels of some cell cycle related genes analyzed by qPCR in SLC 35F2‐ KO group compared to control KTC ‐1 cells. Data were plotted relative to expression levels in control cells (* P

    Article Snippet: The following antibodies were used to explore protein expression: anti‐SLC35F2 antibodies (AV43971, Sigma‐Aldrich), anti‐β‐actin (#4970), anti‐CDK2 (#2546), anti‐CDK4 (#12790), anti‐CDK6 (#13331), anti‐Cyclin D1 (#2978), anti‐Cyclin D3 (#2936), anti‐p27 Kip1 (#3686), anti‐p21 Waf1/Cip1 (#2947), anti‐p18 INK4C (#2896), anti‐ERK1/2 (#4695), anti‐p‐ERK1/2 (Thr202/Tyr204, #4370), anti‐JNK (#9252), anti‐p‐JNK (Thr183/Tyr185, #4668), anti‐p38 MAPK (#8690), anti‐p‐p38 MAPK (Thr180/Tyr182, #4511), anti‐ASK‐1 (#8662), anti‐phosphorylation of apoptosis signal‐regulating kinase 1 (p‐ASK‐1) (Thr845, #3765) (Cell Signaling Technology) and anti‐TGFBR1 (CY2905, Abways, China).

    Techniques: Knock-Out, FACS, Inhibition, Flow Cytometry, Cytometry, Over Expression, Plasmid Preparation, Expressing, Sublimation, Western Blot, Real-time Polymerase Chain Reaction

    Effects of cediranib on olaparib-induced apoptosis and cell cycle progression in EOC cells. (A) PEO1 and PEO4 cells were pre-treated with 0, 2.5, and 5 μM cediranib for 1 hr and then treated with 0, 5, and 10 μM olaparib in the continuous presence of cediranib. After 24 and 48 hr of incubation, cells were lysed, and native protein was obtained to determine caspase 3/7 activity. The protein concentration of lysates was also determined to normalize the caspase 3/7 activity in each sample. The level of apoptosis is expressed as the fold change in the normalized caspase 3/7 activity with respect to the vehicle-treated control in each cell line. (B) PEO1 and PEO4 cells were treated with 0, 2.5, and 5 μM cediranib for 24 hr. Western blot analysis was performed to determine the protein levels of phospho-Rb (Ser780), cyclin A, p27 Kip1, and HSC70. (C) PEO1 and PEO4 cells were treated with 5 μM cediranib for 24 and 48 hr. Cells were pulse-treated with 10 μM EdU for 1 hr prior to flow cytometric analysis. G1, S, G2 populations were gated to show the percentage of cells in each phase. Data are means ± SD. *, p

    Journal: PLoS ONE

    Article Title: Combination of triapine, olaparib, and cediranib suppresses progression of BRCA-wild type and PARP inhibitor-resistant epithelial ovarian cancer

    doi: 10.1371/journal.pone.0207399

    Figure Lengend Snippet: Effects of cediranib on olaparib-induced apoptosis and cell cycle progression in EOC cells. (A) PEO1 and PEO4 cells were pre-treated with 0, 2.5, and 5 μM cediranib for 1 hr and then treated with 0, 5, and 10 μM olaparib in the continuous presence of cediranib. After 24 and 48 hr of incubation, cells were lysed, and native protein was obtained to determine caspase 3/7 activity. The protein concentration of lysates was also determined to normalize the caspase 3/7 activity in each sample. The level of apoptosis is expressed as the fold change in the normalized caspase 3/7 activity with respect to the vehicle-treated control in each cell line. (B) PEO1 and PEO4 cells were treated with 0, 2.5, and 5 μM cediranib for 24 hr. Western blot analysis was performed to determine the protein levels of phospho-Rb (Ser780), cyclin A, p27 Kip1, and HSC70. (C) PEO1 and PEO4 cells were treated with 5 μM cediranib for 24 and 48 hr. Cells were pulse-treated with 10 μM EdU for 1 hr prior to flow cytometric analysis. G1, S, G2 populations were gated to show the percentage of cells in each phase. Data are means ± SD. *, p

    Article Snippet: Phospho-AKT (Ser473), AKT, mTOR, phospho-S6 (Ser235/236), S6, phospho-FoxO1 (Ser248), cyclin A, phospho-Rb (Ser780), Rb, and p27 Kip1 antibodies were purchased from Cell Signaling (Danvers, MA).

    Techniques: Incubation, Activity Assay, Protein Concentration, Western Blot, Flow Cytometry

    PHD3 depletion increases S10 phosphorylation of p27 in hypoxia. a Western blot analysis of p27 expression in cells arrested at different cell cycle phases and exposed to PHD3 or control siRNA. PHD3 depletion has no effect on T187 phosphorylation of p27 at any cell cycle phase. b PHD3 depletion has little effect on p27 phosphorylated on T157 and T198. c S10 phosphorylated form of p27 is strongly induced in PHD3 depleted cells. d Quantification of total and indicated p27 phosphoproteins from four independent experiments normalized to β-actin. Out of the phosphoproteins the effect on the expression of p27S10 is most prominent. Asterisk indicates significant difference ( p

    Journal: Molecular Cancer

    Article Title: Hypoxia inducible prolyl hydroxylase PHD3 maintains carcinoma cell growth by decreasing the stability of p27

    doi: 10.1186/s12943-015-0410-5

    Figure Lengend Snippet: PHD3 depletion increases S10 phosphorylation of p27 in hypoxia. a Western blot analysis of p27 expression in cells arrested at different cell cycle phases and exposed to PHD3 or control siRNA. PHD3 depletion has no effect on T187 phosphorylation of p27 at any cell cycle phase. b PHD3 depletion has little effect on p27 phosphorylated on T157 and T198. c S10 phosphorylated form of p27 is strongly induced in PHD3 depleted cells. d Quantification of total and indicated p27 phosphoproteins from four independent experiments normalized to β-actin. Out of the phosphoproteins the effect on the expression of p27S10 is most prominent. Asterisk indicates significant difference ( p

    Article Snippet: Antibodies used were: PHD3 (NB100-139, Novus Biologicals), PHD2 (NB100-137, Novus Biologicals), PHD1 (NB100-310, Novus Biologicals), Flag (F3165, Sigma-Aldrich), HIF-1α (610959, BD Transduction Laboratories), EPAS1/HIF-2α (NB100-122, Novus Biologicals), p16 (554079, BD Pharmingen/sc-468, Santa Cruz Biotechnology Inc.), p21 (sc-397, Santa Cruz Biotechnology Inc.), p27 (sc-528, Santa Cruz Biotechnology Inc.), p-p27(S10) (sc-12939-R, Santa Cruz Biotechnology Inc.), p-p27(T157) (AF1555, R & D Systems), p-p27(T187) (sc-16324, Santa Cruz Biotechnology Inc.), p-p27(T198) (AF3994, R & D Systems), Skp2 (sc-7164, Santa Cruz Biotechnology Inc.) and β-actin (Ac-74, Sigma-Aldrich).

    Techniques: Western Blot, Expressing

    Effect of lignans on expression of P21 and P27 in RMCs induced by Ang II. β -actin and GAPDH were used as an internal loading control gene. Both mRNA and protein relative expression levels were expressed as folds of control. All values were expressed as mean ± SD ( n = 3). (a) Effect of lignans on mRNA expression of P21 and P27 by RT-qPCR. (b, c1~c2) Effect of lignans on protein expression of P21 and P27 by western blot; Con: control; Ang II: 10 −8 mol/L Ang II group; Epa: 10 −8 mol/L Ang II + 20 μ mol/L epalrestat group; L Lig: 10 −8 mol/L Ang II + 20 mg/L lignan group; M Lig: 10 −8 mol/L Ang II + 40 mg/L lignan group; H Lig: 10 −8 mol/L Ang II + 80 mg/L lignan group; ∗ P

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Eucommia ulmoides Oliv. (Du-Zhong) Lignans Inhibit Angiotensin II-Stimulated Proliferation by Affecting P21, P27, and Bax Expression in Rat Mesangial Cells

    doi: 10.1155/2015/987973

    Figure Lengend Snippet: Effect of lignans on expression of P21 and P27 in RMCs induced by Ang II. β -actin and GAPDH were used as an internal loading control gene. Both mRNA and protein relative expression levels were expressed as folds of control. All values were expressed as mean ± SD ( n = 3). (a) Effect of lignans on mRNA expression of P21 and P27 by RT-qPCR. (b, c1~c2) Effect of lignans on protein expression of P21 and P27 by western blot; Con: control; Ang II: 10 −8 mol/L Ang II group; Epa: 10 −8 mol/L Ang II + 20 μ mol/L epalrestat group; L Lig: 10 −8 mol/L Ang II + 20 mg/L lignan group; M Lig: 10 −8 mol/L Ang II + 40 mg/L lignan group; H Lig: 10 −8 mol/L Ang II + 80 mg/L lignan group; ∗ P

    Article Snippet: Antibodies against P21, P27, Bax, Bcl-2, and AR for western blotting were supplied by Abcam (Cambridge, England) and Santa Cruz (CA, USA).

    Techniques: Expressing, Quantitative RT-PCR, Western Blot

    Humoral immunity at the time of initial low-dose SHIV-1157ipEL-p challenge. (A) Reciprocal serum antibody ELISA titers against SIVmac251 p27 Gag, HIV-1 Tat and heterologous clade C HIV CN54 gp120. (B) NAb activity SHIV-1157ipEL-p and, SHIV SF162P4 ) and Tier 2 (SHIV-1157ipd3N4, SHIV-2873Nip) viruses was measured in human PBMC in the presence of polymyxin B. TZM-bl neutralization assay was also performed against SHIV-1157ipEL-p. IC 50 and IC 90 titers, reciprocal dilutions of serum giving 50% and 90% neutralization (inhibitory concentrations), respectively, are shown. *, Mamu A*001-positive RM.

    Journal: PLoS ONE

    Article Title: Vaccination against Heterologous R5 Clade C SHIV: Prevention of Infection and Correlates of Protection

    doi: 10.1371/journal.pone.0022010

    Figure Lengend Snippet: Humoral immunity at the time of initial low-dose SHIV-1157ipEL-p challenge. (A) Reciprocal serum antibody ELISA titers against SIVmac251 p27 Gag, HIV-1 Tat and heterologous clade C HIV CN54 gp120. (B) NAb activity SHIV-1157ipEL-p and, SHIV SF162P4 ) and Tier 2 (SHIV-1157ipd3N4, SHIV-2873Nip) viruses was measured in human PBMC in the presence of polymyxin B. TZM-bl neutralization assay was also performed against SHIV-1157ipEL-p. IC 50 and IC 90 titers, reciprocal dilutions of serum giving 50% and 90% neutralization (inhibitory concentrations), respectively, are shown. *, Mamu A*001-positive RM.

    Article Snippet: Serum antibody binding titers ELISA plates were coated with SIVmac251 p27 (Immunodiagnostics, Inc., Woburn, MA), HIV-1 Tat and HIVCN54 gp120 (ARRRP), diluted to 2 µg/ml.

    Techniques: Enzyme-linked Immunosorbent Assay, Activity Assay, Neutralization

    p27 knockdown partially rescues MLN4924-induced migration and proliferation, but not tube formation MS1 cells were first transfected with siRNA targeting p27 and si-Cont for 72 hrs, followed by MLN4924 treatment for 24 hrs. One portion was subjected to IB ( A ), and the other portion was used for assays of migration ( B ), proliferation ( C ) and tube formation ( D ). Shown is mean ± SEM from three independent experiments. Scale bar represents 50 μm.

    Journal: Oncogene

    Article Title: Endothelial deletion of Sag/Rbx2/Roc2 E3 ubiquitin ligase causes embryonic lethality and blocks tumor angiogenesis

    doi: 10.1038/onc.2013.473

    Figure Lengend Snippet: p27 knockdown partially rescues MLN4924-induced migration and proliferation, but not tube formation MS1 cells were first transfected with siRNA targeting p27 and si-Cont for 72 hrs, followed by MLN4924 treatment for 24 hrs. One portion was subjected to IB ( A ), and the other portion was used for assays of migration ( B ), proliferation ( C ) and tube formation ( D ). Shown is mean ± SEM from three independent experiments. Scale bar represents 50 μm.

    Article Snippet: The sequence for these siRNA oligonucleotides are as follows: Si-Cont: 5′-AUUGUAUGCGA UCGCAGAC-3′; and Si-p27 (pooled from Santa Cruz Biotechnology).

    Techniques: Migration, Transfection

    p27 deletion partially rescues Sag deletion-induced defects in migration and proliferation, but not tube formation MS1 cells were infected with Lt-Sag and Lt-Cont and co-transfected with siRNA oligonucleotides targeting p27, along with scrambled control siRNA for 72 hrs. One portion was subjected to IB ( A ), and the other portion was used for assays of migration (B), proliferation ( C ) and tube formation ( D ). Shown is mean ± SEM from three independent experiments. Scale bar represents 50 μm.

    Journal: Oncogene

    Article Title: Endothelial deletion of Sag/Rbx2/Roc2 E3 ubiquitin ligase causes embryonic lethality and blocks tumor angiogenesis

    doi: 10.1038/onc.2013.473

    Figure Lengend Snippet: p27 deletion partially rescues Sag deletion-induced defects in migration and proliferation, but not tube formation MS1 cells were infected with Lt-Sag and Lt-Cont and co-transfected with siRNA oligonucleotides targeting p27, along with scrambled control siRNA for 72 hrs. One portion was subjected to IB ( A ), and the other portion was used for assays of migration (B), proliferation ( C ) and tube formation ( D ). Shown is mean ± SEM from three independent experiments. Scale bar represents 50 μm.

    Article Snippet: The sequence for these siRNA oligonucleotides are as follows: Si-Cont: 5′-AUUGUAUGCGA UCGCAGAC-3′; and Si-p27 (pooled from Santa Cruz Biotechnology).

    Techniques: Migration, Infection, Transfection