c. cloning Search Results


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  • 95
    Millipore anti c myc clone 9e10 antibodies
    Anti C Myc Clone 9e10 Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Thermo Fisher c his topo cloning kit
    C His Topo Cloning Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alicator lic cloning and expression kit 3
    Alicator Lic Cloning And Expression Kit 3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher instaclone pcr c loning kit
    Instaclone Pcr C Loning Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    OriGene lentivirus delivered pgfp c shlenti shrna cloning plasmid
    Lentivirus Delivered Pgfp C Shlenti Shrna Cloning Plasmid, supplied by OriGene, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Integrated DNA Technologies dideoxy c base cloning linker 5rapp ctgtaggcaccatcaat 3ddc
    Dideoxy C Base Cloning Linker 5rapp Ctgtaggcaccatcaat 3ddc, supplied by Integrated DNA Technologies, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher monoclonal anti c myc antibody
    WNT-dependent phosphorylation of the <t>DVL2</t> mutant protein is reduced. (A) Lysates from NIH/3T3 stable cell lines expressing the dog, Myc-tagged wild-type (Wt) or mutant variant (Mut) DVL2, which is 23 aa shorter than wild-type exogenous DVL2, were analyzed by western blotting using an <t>anti-c-Myc</t> antibody. To assess the ability of the wild-type and mutant proteins to respond to WNT stimulation, cells were treated with WNT5A or WNT3A for 6 hours. Both treatments resulted in increased gel mobility shifts of the wild-type DVL2 protein, indicative of increased phosphorylation; this effect was reduced on the mutant DVL2 protein. (B) To confirm that the DVL2 gel mobility shifts observed in (A) were due to phosphorylation, cell lysates were subjected to mock treatment (30 min incubation at 37 C), or calf intestinal phosphatase (CIP) treatment (30 min incubation at 37 C in the presence of CIP) before separation by SDS-PAGE. The DVL2 gel mobility shifts above wild-type and mutant proteins were lost after CIP treatment, confirming that they are caused by phosphorylation. (C) To test whether the DVL2 gel mobility shifts observed in (A) were driven by casein kinase 1 (CK1), cells were treated with D4476, a CK1 inhibitor, for 1 hour prior to and concurrently during the Wnt stimulation for 6 hours. The DVL2 gel mobility shifts were lost after D4476 treatment, further indicating that they are caused by CK1-dependent phosphorylation. α-tubulin was used for loading controls. Cell lysates were normalized by BCA assays for total protein.
    Monoclonal Anti C Myc Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher topo ta cloning kit version c
    WNT-dependent phosphorylation of the <t>DVL2</t> mutant protein is reduced. (A) Lysates from NIH/3T3 stable cell lines expressing the dog, Myc-tagged wild-type (Wt) or mutant variant (Mut) DVL2, which is 23 aa shorter than wild-type exogenous DVL2, were analyzed by western blotting using an <t>anti-c-Myc</t> antibody. To assess the ability of the wild-type and mutant proteins to respond to WNT stimulation, cells were treated with WNT5A or WNT3A for 6 hours. Both treatments resulted in increased gel mobility shifts of the wild-type DVL2 protein, indicative of increased phosphorylation; this effect was reduced on the mutant DVL2 protein. (B) To confirm that the DVL2 gel mobility shifts observed in (A) were due to phosphorylation, cell lysates were subjected to mock treatment (30 min incubation at 37 C), or calf intestinal phosphatase (CIP) treatment (30 min incubation at 37 C in the presence of CIP) before separation by SDS-PAGE. The DVL2 gel mobility shifts above wild-type and mutant proteins were lost after CIP treatment, confirming that they are caused by phosphorylation. (C) To test whether the DVL2 gel mobility shifts observed in (A) were driven by casein kinase 1 (CK1), cells were treated with D4476, a CK1 inhibitor, for 1 hour prior to and concurrently during the Wnt stimulation for 6 hours. The DVL2 gel mobility shifts were lost after D4476 treatment, further indicating that they are caused by CK1-dependent phosphorylation. α-tubulin was used for loading controls. Cell lysates were normalized by BCA assays for total protein.
    Topo Ta Cloning Kit Version C, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    OriGene fast skeletal mybp c clones
    3D reconstruction of thin filaments demonstrates <t>MyBP-C</t> N-termini shift of tropomyosin in the absence of Ca 2+ . ( A ) Reconstruction of reconstituted thin filament (F-actin, tropomyosin, troponin). Actin atomic structure (yellow ribbon) has been fitted into the reconstruction (grey envelope). Red and green helices represent Tm in the known blocked and closed positions on the thin filament, respectively. In this control filament, at low Ca 2+ , Tm occupies the blocked position (grey cylinder enclosing red Tm helix). Tn is averaged out as it does not follow the helical symmetry of actin used to carry out the reconstructions. The addition of ( B ) ssC1C2, ( C ) fsC1C2, and ( D ) C0C2 causes a shift in Tm azimuth towards the closed position, with C0C2 causing the largest shift and fsC1C2 the smallest. These variable shifts are further revealed when each decorated reconstruction is superimposed on the actin:tropomyosin:troponin control, both in surface view ( E – H ) and in cross-sectional views of the reconstructions ( I – O ) ( cf . ref. 14 ). Actin subdomains 1–4 are marked in I . Red arrows indicate Tm in blocked position in low Ca 2+ control filament; green arrows show shifted position of Tm in low Ca 2+ decorated filaments.
    Fast Skeletal Mybp C Clones, supplied by OriGene, used in various techniques. Bioz Stars score: 99/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    BioVision c peptide
    3D reconstruction of thin filaments demonstrates <t>MyBP-C</t> N-termini shift of tropomyosin in the absence of Ca 2+ . ( A ) Reconstruction of reconstituted thin filament (F-actin, tropomyosin, troponin). Actin atomic structure (yellow ribbon) has been fitted into the reconstruction (grey envelope). Red and green helices represent Tm in the known blocked and closed positions on the thin filament, respectively. In this control filament, at low Ca 2+ , Tm occupies the blocked position (grey cylinder enclosing red Tm helix). Tn is averaged out as it does not follow the helical symmetry of actin used to carry out the reconstructions. The addition of ( B ) ssC1C2, ( C ) fsC1C2, and ( D ) C0C2 causes a shift in Tm azimuth towards the closed position, with C0C2 causing the largest shift and fsC1C2 the smallest. These variable shifts are further revealed when each decorated reconstruction is superimposed on the actin:tropomyosin:troponin control, both in surface view ( E – H ) and in cross-sectional views of the reconstructions ( I – O ) ( cf . ref. 14 ). Actin subdomains 1–4 are marked in I . Red arrows indicate Tm in blocked position in low Ca 2+ control filament; green arrows show shifted position of Tm in low Ca 2+ decorated filaments.
    C Peptide, supplied by BioVision, used in various techniques. Bioz Stars score: 76/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Thermo Fisher anti tcr c gamma m1 clone
    3D reconstruction of thin filaments demonstrates <t>MyBP-C</t> N-termini shift of tropomyosin in the absence of Ca 2+ . ( A ) Reconstruction of reconstituted thin filament (F-actin, tropomyosin, troponin). Actin atomic structure (yellow ribbon) has been fitted into the reconstruction (grey envelope). Red and green helices represent Tm in the known blocked and closed positions on the thin filament, respectively. In this control filament, at low Ca 2+ , Tm occupies the blocked position (grey cylinder enclosing red Tm helix). Tn is averaged out as it does not follow the helical symmetry of actin used to carry out the reconstructions. The addition of ( B ) ssC1C2, ( C ) fsC1C2, and ( D ) C0C2 causes a shift in Tm azimuth towards the closed position, with C0C2 causing the largest shift and fsC1C2 the smallest. These variable shifts are further revealed when each decorated reconstruction is superimposed on the actin:tropomyosin:troponin control, both in surface view ( E – H ) and in cross-sectional views of the reconstructions ( I – O ) ( cf . ref. 14 ). Actin subdomains 1–4 are marked in I . Red arrows indicate Tm in blocked position in low Ca 2+ control filament; green arrows show shifted position of Tm in low Ca 2+ decorated filaments.
    Anti Tcr C Gamma M1 Clone, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    BioVision cytochrome c antibody
    Expression of Bcl-2, Bax, Survivin, ERK, cytochrome C, Caspase-3 and VEGF in 4T1 cells after 48 h treatment of fucoidan detected by Western blot. Expression of the β-actin gene was used as the internal control. Data are mean±SD of one representative experiment performed in triplicate. Fucoidan significantly decreased the expression of Bcl-2, did not modulate the expression of Bax, but the ratio Bcl-2/Bax was decreased. Fucoidan also decreased the protein expression of Survivin and phosphorylated ERKs in 4T1 cells. Fucoidan treatment significantly increased levels of <t>cytochrome</t> C in the cytoplasm, whereas there was a significant corresponding decline of mitochondrial cytochrome C. Cytochrome oxidase (subunit II) was as sample loading control (cyt. oxid). The level of pro-caspase-3 decreased after fucoidan treatment, while the level of caspase-3 cleavage protein increased after fucoidan treatment. Fucoidan decreased VEGF expression in 4T1 cells. Lane 1: control cells; lanes 2–4: 4T1 cells treated with 50, 100 and 200 μg/ml fucoidan respectively. * P
    Cytochrome C Antibody, supplied by BioVision, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher c jun specific shrna clones
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Jun Specific Shrna Clones, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher c kit rp23 274l11 bac clones
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Kit Rp23 274l11 Bac Clones, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti c kit clone h300 antibodies
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Anti C Kit Clone H300 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology actin clone c 11 antibodies
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Actin Clone C 11 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 84/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti pkcδ clone c 20 antibodies
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Anti Pkcδ Clone C 20 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 81/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance c myc clone 9e10 antibodies
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Myc Clone 9e10 Antibodies, supplied by Covance, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    System Biosciences Inc c clones mir 124 overexpressing lentivirus
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Clones Mir 124 Overexpressing Lentivirus, supplied by System Biosciences Inc, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam mouse monoclonal anti c src antibody
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Mouse Monoclonal Anti C Src Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 87/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher anti creb clone
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Anti Creb Clone, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti c myc clone 9e10 antibodies
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    Anti C Myc Clone 9e10 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Source BioScience plc c elegans feeding rnai clones
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Elegans Feeding Rnai Clones, supplied by Source BioScience plc, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Source BioScience plc c elegans fosmid library clones
    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or <t>siRNA</t> specific for PDK1 were analyzed by Western
    C Elegans Fosmid Library Clones, supplied by Source BioScience plc, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Agilent technologies c pan mhc class i w6 32 clone pe
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    C Pan Mhc Class I W6 32 Clone Pe, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    R&D Systems mouse anti tenascin c clone t2h5 antibodies
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    Mouse Anti Tenascin C Clone T2h5 Antibodies, supplied by R&D Systems, used in various techniques. Bioz Stars score: 81/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti c ebp β clone h7 monoclonal antibody
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    Anti C Ebp β Clone H7 Monoclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Sino Biological cystatin c cdna cloning vector
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    Cystatin C Cdna Cloning Vector, supplied by Sino Biological, used in various techniques. Bioz Stars score: 89/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher cd117 c kit clone 104d2 conjugated
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    Cd117 C Kit Clone 104d2 Conjugated, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Cedarlane anti rat cd11b c purified clone ox 42 mouse igg2a
    CVB4 E2 infection upregulates <t>MHC</t> class I. (A and B) MHC <t>class</t> I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.
    Anti Rat Cd11b C Purified Clone Ox 42 Mouse Igg2a, supplied by Cedarlane, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    WNT-dependent phosphorylation of the DVL2 mutant protein is reduced. (A) Lysates from NIH/3T3 stable cell lines expressing the dog, Myc-tagged wild-type (Wt) or mutant variant (Mut) DVL2, which is 23 aa shorter than wild-type exogenous DVL2, were analyzed by western blotting using an anti-c-Myc antibody. To assess the ability of the wild-type and mutant proteins to respond to WNT stimulation, cells were treated with WNT5A or WNT3A for 6 hours. Both treatments resulted in increased gel mobility shifts of the wild-type DVL2 protein, indicative of increased phosphorylation; this effect was reduced on the mutant DVL2 protein. (B) To confirm that the DVL2 gel mobility shifts observed in (A) were due to phosphorylation, cell lysates were subjected to mock treatment (30 min incubation at 37 C), or calf intestinal phosphatase (CIP) treatment (30 min incubation at 37 C in the presence of CIP) before separation by SDS-PAGE. The DVL2 gel mobility shifts above wild-type and mutant proteins were lost after CIP treatment, confirming that they are caused by phosphorylation. (C) To test whether the DVL2 gel mobility shifts observed in (A) were driven by casein kinase 1 (CK1), cells were treated with D4476, a CK1 inhibitor, for 1 hour prior to and concurrently during the Wnt stimulation for 6 hours. The DVL2 gel mobility shifts were lost after D4476 treatment, further indicating that they are caused by CK1-dependent phosphorylation. α-tubulin was used for loading controls. Cell lysates were normalized by BCA assays for total protein.

    Journal: PLoS Genetics

    Article Title: Whole genome variant association across 100 dogs identifies a frame shift mutation in DISHEVELLED 2 which contributes to Robinow-like syndrome in Bulldogs and related screw tail dog breeds

    doi: 10.1371/journal.pgen.1007850

    Figure Lengend Snippet: WNT-dependent phosphorylation of the DVL2 mutant protein is reduced. (A) Lysates from NIH/3T3 stable cell lines expressing the dog, Myc-tagged wild-type (Wt) or mutant variant (Mut) DVL2, which is 23 aa shorter than wild-type exogenous DVL2, were analyzed by western blotting using an anti-c-Myc antibody. To assess the ability of the wild-type and mutant proteins to respond to WNT stimulation, cells were treated with WNT5A or WNT3A for 6 hours. Both treatments resulted in increased gel mobility shifts of the wild-type DVL2 protein, indicative of increased phosphorylation; this effect was reduced on the mutant DVL2 protein. (B) To confirm that the DVL2 gel mobility shifts observed in (A) were due to phosphorylation, cell lysates were subjected to mock treatment (30 min incubation at 37 C), or calf intestinal phosphatase (CIP) treatment (30 min incubation at 37 C in the presence of CIP) before separation by SDS-PAGE. The DVL2 gel mobility shifts above wild-type and mutant proteins were lost after CIP treatment, confirming that they are caused by phosphorylation. (C) To test whether the DVL2 gel mobility shifts observed in (A) were driven by casein kinase 1 (CK1), cells were treated with D4476, a CK1 inhibitor, for 1 hour prior to and concurrently during the Wnt stimulation for 6 hours. The DVL2 gel mobility shifts were lost after D4476 treatment, further indicating that they are caused by CK1-dependent phosphorylation. α-tubulin was used for loading controls. Cell lysates were normalized by BCA assays for total protein.

    Article Snippet: For detecting exogenous DVL2, a commercially purchased monoclonal anti-c-Myc antibody (clone 9E10, Thermo Fisher Scientific, catalog #9801) was used as the primary antibody at a dilution ratio of 1/1000, and a goat anti-rabbit IgG polyclonal antibody (conjugated to IRDye 800CW; catalog # 926–32211, Li-cor Biosciences, Lincoln, NE) was used as the secondary antibody at a dilution ratio of 1/30,000.

    Techniques: Mutagenesis, Stable Transfection, Expressing, Variant Assay, Western Blot, Incubation, SDS Page, BIA-KA

    3D reconstruction of thin filaments demonstrates MyBP-C N-termini shift of tropomyosin in the absence of Ca 2+ . ( A ) Reconstruction of reconstituted thin filament (F-actin, tropomyosin, troponin). Actin atomic structure (yellow ribbon) has been fitted into the reconstruction (grey envelope). Red and green helices represent Tm in the known blocked and closed positions on the thin filament, respectively. In this control filament, at low Ca 2+ , Tm occupies the blocked position (grey cylinder enclosing red Tm helix). Tn is averaged out as it does not follow the helical symmetry of actin used to carry out the reconstructions. The addition of ( B ) ssC1C2, ( C ) fsC1C2, and ( D ) C0C2 causes a shift in Tm azimuth towards the closed position, with C0C2 causing the largest shift and fsC1C2 the smallest. These variable shifts are further revealed when each decorated reconstruction is superimposed on the actin:tropomyosin:troponin control, both in surface view ( E – H ) and in cross-sectional views of the reconstructions ( I – O ) ( cf . ref. 14 ). Actin subdomains 1–4 are marked in I . Red arrows indicate Tm in blocked position in low Ca 2+ control filament; green arrows show shifted position of Tm in low Ca 2+ decorated filaments.

    Journal: Scientific Reports

    Article Title: Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner

    doi: 10.1038/s41598-018-21053-1

    Figure Lengend Snippet: 3D reconstruction of thin filaments demonstrates MyBP-C N-termini shift of tropomyosin in the absence of Ca 2+ . ( A ) Reconstruction of reconstituted thin filament (F-actin, tropomyosin, troponin). Actin atomic structure (yellow ribbon) has been fitted into the reconstruction (grey envelope). Red and green helices represent Tm in the known blocked and closed positions on the thin filament, respectively. In this control filament, at low Ca 2+ , Tm occupies the blocked position (grey cylinder enclosing red Tm helix). Tn is averaged out as it does not follow the helical symmetry of actin used to carry out the reconstructions. The addition of ( B ) ssC1C2, ( C ) fsC1C2, and ( D ) C0C2 causes a shift in Tm azimuth towards the closed position, with C0C2 causing the largest shift and fsC1C2 the smallest. These variable shifts are further revealed when each decorated reconstruction is superimposed on the actin:tropomyosin:troponin control, both in surface view ( E – H ) and in cross-sectional views of the reconstructions ( I – O ) ( cf . ref. 14 ). Actin subdomains 1–4 are marked in I . Red arrows indicate Tm in blocked position in low Ca 2+ control filament; green arrows show shifted position of Tm in low Ca 2+ decorated filaments.

    Article Snippet: Adenovirus Infection and Cell Culture Commercially purchased slow- and fast-skeletal MyBP-C clones from Origene (NM_175418.3 and NM_004533, Rockville, MD) were used to construct the adenoviruses overexpressing skeletal isoforms of MyBP-C. cMyBP-C adenoviral vectors were generated by the core facilities at Loyola University Chicago.

    Techniques:

    Regulation of muscle contraction by MyBP-C isoforms was determined using recombinant proteins representing the N-terminal region of slow-skeletal, fast-skeletal, and cardiac isoforms of MyBP-C. ( A ) Schematic diagram of full-length slow-skeletal, fast-skeletal, and cardiac MyBP-C isoforms (ssMyBP-C, fsMyBP-C, and cMyBP-C, respectively). Domains are numbered C0 to C10 from the N-terminus, and proline-alanine region (PA) is common to all isoforms. Circles denote immunoglobulin-like domains, and pentagons represent fibronectin type 3 domains. Yellow lines identify known phosphorylation sites; red lines indicate cardiac-specific insert in C5 domain of cMyBP-C. ( B ) SDS-PAGE demonstrates the relative size and purity of each MyBP-C recombinant protein, encompassing the N-terminal region, up to and including the C2 domain. ( C – F ) Permeabilized ventricular rat papillary muscles were left untreated (control, white column) or were incubated with 10 µM ssC1C2 (red), fsC1C2 (blue), and C0C2 (black) and allowed to undergo muscle contraction analysis by the Force-ATPase assay. ( C ) Relative force-pCa curves and ( D ) quantification of pCa 50 values from the relative force-pCa curves demonstrate significant increases of fsC1C2 and C0C2 in Ca 2+ -sensitivity of force development. ( E ) Rate of tension redevelopment ( k tr ) was determined using a rapid release and restretch maneuver at maximal Ca 2+ levels (pCa 4.5) and submaximal Ca 2+ levels (pCa 6). Top trace is of ( F ) at pCa 6, and k tr was significantly enhanced by fsC1C2 and C0C2. Graphs represented as mean ± SEM, *p

    Journal: Scientific Reports

    Article Title: Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner

    doi: 10.1038/s41598-018-21053-1

    Figure Lengend Snippet: Regulation of muscle contraction by MyBP-C isoforms was determined using recombinant proteins representing the N-terminal region of slow-skeletal, fast-skeletal, and cardiac isoforms of MyBP-C. ( A ) Schematic diagram of full-length slow-skeletal, fast-skeletal, and cardiac MyBP-C isoforms (ssMyBP-C, fsMyBP-C, and cMyBP-C, respectively). Domains are numbered C0 to C10 from the N-terminus, and proline-alanine region (PA) is common to all isoforms. Circles denote immunoglobulin-like domains, and pentagons represent fibronectin type 3 domains. Yellow lines identify known phosphorylation sites; red lines indicate cardiac-specific insert in C5 domain of cMyBP-C. ( B ) SDS-PAGE demonstrates the relative size and purity of each MyBP-C recombinant protein, encompassing the N-terminal region, up to and including the C2 domain. ( C – F ) Permeabilized ventricular rat papillary muscles were left untreated (control, white column) or were incubated with 10 µM ssC1C2 (red), fsC1C2 (blue), and C0C2 (black) and allowed to undergo muscle contraction analysis by the Force-ATPase assay. ( C ) Relative force-pCa curves and ( D ) quantification of pCa 50 values from the relative force-pCa curves demonstrate significant increases of fsC1C2 and C0C2 in Ca 2+ -sensitivity of force development. ( E ) Rate of tension redevelopment ( k tr ) was determined using a rapid release and restretch maneuver at maximal Ca 2+ levels (pCa 4.5) and submaximal Ca 2+ levels (pCa 6). Top trace is of ( F ) at pCa 6, and k tr was significantly enhanced by fsC1C2 and C0C2. Graphs represented as mean ± SEM, *p

    Article Snippet: Adenovirus Infection and Cell Culture Commercially purchased slow- and fast-skeletal MyBP-C clones from Origene (NM_175418.3 and NM_004533, Rockville, MD) were used to construct the adenoviruses overexpressing skeletal isoforms of MyBP-C. cMyBP-C adenoviral vectors were generated by the core facilities at Loyola University Chicago.

    Techniques: Recombinant, SDS Page, Incubation, ATPase Assay

    Greater activation of thin filament results in prolonged diastole. ( A ) To determine how each isoform regulates dynamic contraction, full-length MyBP-C adult rat ventricular myocytes (ARVM) were infected with adenoviral constructs (MOI 1000) overexpressing full-length, cMyc-tagged slow-skeletal, fast-skeletal, or cardiac MyBP-C, followed by 48 h culture. ( B ) Immunofluorescence (IF) imaging demonstrates localization of adenoviral-mediated expression of MyBP-C isoforms (green) within the sarcomere, as delineated by α-actinin (red). ( C , D ) Unloaded shortening was measured by changes in sarcomere length (SL) during dynamic contraction and relaxation (ARVM paced at 1 Hz, 20 V, 2 ms). ( C ) Relaxation kinetics was measured by time to % baseline, how fast the cell returns to 10, 50, and 90% of resting SL, and ( D ) relaxation constant tau, a logarithmic fit of the relaxation curve. ( E ) Changes in relaxation kinetics were evident by combined traces, and in silico simulations demonstrate that greater thin filament activation can contribute to relaxation kinetics. Graphs represented as mean ± SEM, *p

    Journal: Scientific Reports

    Article Title: Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner

    doi: 10.1038/s41598-018-21053-1

    Figure Lengend Snippet: Greater activation of thin filament results in prolonged diastole. ( A ) To determine how each isoform regulates dynamic contraction, full-length MyBP-C adult rat ventricular myocytes (ARVM) were infected with adenoviral constructs (MOI 1000) overexpressing full-length, cMyc-tagged slow-skeletal, fast-skeletal, or cardiac MyBP-C, followed by 48 h culture. ( B ) Immunofluorescence (IF) imaging demonstrates localization of adenoviral-mediated expression of MyBP-C isoforms (green) within the sarcomere, as delineated by α-actinin (red). ( C , D ) Unloaded shortening was measured by changes in sarcomere length (SL) during dynamic contraction and relaxation (ARVM paced at 1 Hz, 20 V, 2 ms). ( C ) Relaxation kinetics was measured by time to % baseline, how fast the cell returns to 10, 50, and 90% of resting SL, and ( D ) relaxation constant tau, a logarithmic fit of the relaxation curve. ( E ) Changes in relaxation kinetics were evident by combined traces, and in silico simulations demonstrate that greater thin filament activation can contribute to relaxation kinetics. Graphs represented as mean ± SEM, *p

    Article Snippet: Adenovirus Infection and Cell Culture Commercially purchased slow- and fast-skeletal MyBP-C clones from Origene (NM_175418.3 and NM_004533, Rockville, MD) were used to construct the adenoviruses overexpressing skeletal isoforms of MyBP-C. cMyBP-C adenoviral vectors were generated by the core facilities at Loyola University Chicago.

    Techniques: Activation Assay, Infection, Construct, Immunofluorescence, Imaging, Expressing, Mass Spectrometry, In Silico

    In vitro motility assays demonstrate MyBP-C regulation by promoting and inhibiting motility of native thin filaments (NTFs) at low and high Ca 2+ , respectively. ( A – C ) Control NTFs (grey line) show a sigmoidal increase in activation in response to increasing calcium levels. C0C2, fsC1C2, and ssC1C2 (0.25 µM) all shift this response to the left, indicating an increased activation effect at lower Ca 2+ levels. ( A ) C0C2 activates NTF sliding velocities at both low Ca 2+ levels and inhibits NTF motility at high Ca 2+ levels. ( B ) fsC1C2 is unable to activate NTF motility at low Ca 2+ levels, but inhibits NTF motility at higher Ca 2+ levels. ( C ) Conversely, ssC1C2 activates NTF motility at low Ca 2+ levels, but lacks the capacity to limit NTF motility at high Ca 2+ levels. Effects of MyBP-C N-termini varied, depending on concentration, as demonstrated by dose-dependent responses of C0C2, fsC1C2, and ssC1C2 on NTF motility at ( D ) pCa 9 ( E ) pCa 6.75 and ( F ) pCa 5. Graphs represented as mean ± SEM.

    Journal: Scientific Reports

    Article Title: Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner

    doi: 10.1038/s41598-018-21053-1

    Figure Lengend Snippet: In vitro motility assays demonstrate MyBP-C regulation by promoting and inhibiting motility of native thin filaments (NTFs) at low and high Ca 2+ , respectively. ( A – C ) Control NTFs (grey line) show a sigmoidal increase in activation in response to increasing calcium levels. C0C2, fsC1C2, and ssC1C2 (0.25 µM) all shift this response to the left, indicating an increased activation effect at lower Ca 2+ levels. ( A ) C0C2 activates NTF sliding velocities at both low Ca 2+ levels and inhibits NTF motility at high Ca 2+ levels. ( B ) fsC1C2 is unable to activate NTF motility at low Ca 2+ levels, but inhibits NTF motility at higher Ca 2+ levels. ( C ) Conversely, ssC1C2 activates NTF motility at low Ca 2+ levels, but lacks the capacity to limit NTF motility at high Ca 2+ levels. Effects of MyBP-C N-termini varied, depending on concentration, as demonstrated by dose-dependent responses of C0C2, fsC1C2, and ssC1C2 on NTF motility at ( D ) pCa 9 ( E ) pCa 6.75 and ( F ) pCa 5. Graphs represented as mean ± SEM.

    Article Snippet: Adenovirus Infection and Cell Culture Commercially purchased slow- and fast-skeletal MyBP-C clones from Origene (NM_175418.3 and NM_004533, Rockville, MD) were used to construct the adenoviruses overexpressing skeletal isoforms of MyBP-C. cMyBP-C adenoviral vectors were generated by the core facilities at Loyola University Chicago.

    Techniques: In Vitro, Activation Assay, Concentration Assay

    Expression of Bcl-2, Bax, Survivin, ERK, cytochrome C, Caspase-3 and VEGF in 4T1 cells after 48 h treatment of fucoidan detected by Western blot. Expression of the β-actin gene was used as the internal control. Data are mean±SD of one representative experiment performed in triplicate. Fucoidan significantly decreased the expression of Bcl-2, did not modulate the expression of Bax, but the ratio Bcl-2/Bax was decreased. Fucoidan also decreased the protein expression of Survivin and phosphorylated ERKs in 4T1 cells. Fucoidan treatment significantly increased levels of cytochrome C in the cytoplasm, whereas there was a significant corresponding decline of mitochondrial cytochrome C. Cytochrome oxidase (subunit II) was as sample loading control (cyt. oxid). The level of pro-caspase-3 decreased after fucoidan treatment, while the level of caspase-3 cleavage protein increased after fucoidan treatment. Fucoidan decreased VEGF expression in 4T1 cells. Lane 1: control cells; lanes 2–4: 4T1 cells treated with 50, 100 and 200 μg/ml fucoidan respectively. * P

    Journal: PLoS ONE

    Article Title: Anticancer Properties and Mechanisms of Fucoidan on Mouse Breast Cancer In Vitro and In Vivo

    doi: 10.1371/journal.pone.0043483

    Figure Lengend Snippet: Expression of Bcl-2, Bax, Survivin, ERK, cytochrome C, Caspase-3 and VEGF in 4T1 cells after 48 h treatment of fucoidan detected by Western blot. Expression of the β-actin gene was used as the internal control. Data are mean±SD of one representative experiment performed in triplicate. Fucoidan significantly decreased the expression of Bcl-2, did not modulate the expression of Bax, but the ratio Bcl-2/Bax was decreased. Fucoidan also decreased the protein expression of Survivin and phosphorylated ERKs in 4T1 cells. Fucoidan treatment significantly increased levels of cytochrome C in the cytoplasm, whereas there was a significant corresponding decline of mitochondrial cytochrome C. Cytochrome oxidase (subunit II) was as sample loading control (cyt. oxid). The level of pro-caspase-3 decreased after fucoidan treatment, while the level of caspase-3 cleavage protein increased after fucoidan treatment. Fucoidan decreased VEGF expression in 4T1 cells. Lane 1: control cells; lanes 2–4: 4T1 cells treated with 50, 100 and 200 μg/ml fucoidan respectively. * P

    Article Snippet: Then western blot proceeded with cytochrome C antibody (Biovision).

    Techniques: Expressing, Western Blot

    c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or siRNA specific for PDK1 were analyzed by Western

    Journal: The Journal of Biological Chemistry

    Article Title: c-Jun Regulates Phosphoinositide-dependent Kinase 1 Transcription

    doi: 10.1074/jbc.M109.075630

    Figure Lengend Snippet: c-Jun regulates Akt activity via PDK1. A , PDK1 is required for Akt phosphorylation and activation. Protein extracts (40 μg) from Lu1205 cells transfected with scrambled ( sc ) oligonucleotides or siRNA specific for PDK1 were analyzed by Western

    Article Snippet: siCONTROL (scrambled) and PDK1-specific SMARTpool reagents were used (Dharmacon). c-Jun-specific siRNA oligonucleotide was obtained from Qiagen, and Sp1-specific and Ets-1-specific siRNA oligonucleotides from Ambion. c-Jun-specific shRNA clones were obtained from Open Biosystems.

    Techniques: Activity Assay, Activation Assay, Transfection, Western Blot

    CVB4 E2 infection upregulates MHC class I. (A and B) MHC class I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.

    Journal: Journal of Virology

    Article Title: Coxsackievirus B4 Infection of Human Fetal Thymus Cells

    doi: 10.1128/JVI.78.18.9854-9861.2004

    Figure Lengend Snippet: CVB4 E2 infection upregulates MHC class I. (A and B) MHC class I mean fluorescence intensity (MFI) of DP thymocytes 7 days after inoculation with CVB4 E2 in the absence (A) or presence (B) of CVB4-neutralizing antiserum. Representative data from five experiments are shown.

    Article Snippet: Four-color FACS staining was performed with the indicated combinations of the following antibodies to CD4-allophycocyanin (APC) (Caltag, Burlingame, Calif.); CD8-peridinin chlorophyll protein (PerCP) and CD3-phycoerythrin (PE) (both from BD Bioscience, San Jose, Calif.); HLA-A, -B, and -C (pan-MHC class I, W6/32 clone)-PE (Dako, Carpinteria, Calif.); cytokeratin-fluorescein isothiocyanate (cytokeratin-FITC, clone J1B3; Immunotech, Marseille, France); CD11c-APC and CD8α-PerCP (both from BD Bioscience); and blood dendritic cell A-2-APC (BDCA-2; Miltenyi Biotech, Auburn, Calif.).

    Techniques: Infection, Fluorescence

    Positive correlation between MHC class I upregulation and CVB4 E2 replication in human thymus. (A to C) MHC class I mean fluorescence intensity (MFI) on DP thymocytes versus production of positive-strand (A) and negative-strand (B) CVB4 E2 RNA and infectious virus (C) in FTOC 7 days after CVB4 inoculation.

    Journal: Journal of Virology

    Article Title: Coxsackievirus B4 Infection of Human Fetal Thymus Cells

    doi: 10.1128/JVI.78.18.9854-9861.2004

    Figure Lengend Snippet: Positive correlation between MHC class I upregulation and CVB4 E2 replication in human thymus. (A to C) MHC class I mean fluorescence intensity (MFI) on DP thymocytes versus production of positive-strand (A) and negative-strand (B) CVB4 E2 RNA and infectious virus (C) in FTOC 7 days after CVB4 inoculation.

    Article Snippet: Four-color FACS staining was performed with the indicated combinations of the following antibodies to CD4-allophycocyanin (APC) (Caltag, Burlingame, Calif.); CD8-peridinin chlorophyll protein (PerCP) and CD3-phycoerythrin (PE) (both from BD Bioscience, San Jose, Calif.); HLA-A, -B, and -C (pan-MHC class I, W6/32 clone)-PE (Dako, Carpinteria, Calif.); cytokeratin-fluorescein isothiocyanate (cytokeratin-FITC, clone J1B3; Immunotech, Marseille, France); CD11c-APC and CD8α-PerCP (both from BD Bioscience); and blood dendritic cell A-2-APC (BDCA-2; Miltenyi Biotech, Auburn, Calif.).

    Techniques: Fluorescence