bsa Thermo Fisher Search Results


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  • 90
    Thermo Fisher bovine serum albumin bsa
    Comparison of in vitro experimental data with flow, fit to the diffusion-only and diffusion-convection models. A series of experimental fluorescence recovery curves for <t>FITC-BSA</t> and FITC-2000 kDa dextran were taken over a wide range of known flow
    Bovine Serum Albumin Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 7617 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher maleimide activated bovine serum album
    Comparison of in vitro experimental data with flow, fit to the diffusion-only and diffusion-convection models. A series of experimental fluorescence recovery curves for <t>FITC-BSA</t> and FITC-2000 kDa dextran were taken over a wide range of known flow
    Maleimide Activated Bovine Serum Album, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher bsa
    GAL efficiently labels Gal and GalNAc residues on cell surface glycoproteins. ( A ) Asialo-K20 cells were incubated in <t>PBS</t> with 5 mg/mL <t>BSA,</t> pH 6.7, containing 250 μM aminooxy-biotin in the presence or absence of 10 mM aniline and 50 U/mL galactose
    Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 25730 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Thermo Fisher bsa dpbs
    GAL efficiently labels Gal and GalNAc residues on cell surface glycoproteins. ( A ) Asialo-K20 cells were incubated in <t>PBS</t> with 5 mg/mL <t>BSA,</t> pH 6.7, containing 250 μM aminooxy-biotin in the presence or absence of 10 mM aniline and 50 U/mL galactose
    Bsa Dpbs, supplied by Thermo Fisher, 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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    99
    Thermo Fisher dq bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Dq Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 250 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher bsa kit
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Bsa Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    75
    Thermo Fisher dnp25 bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Dnp25 Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher dnp30 bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Dnp30 Bsa, 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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    90
    Thermo Fisher bsa af593
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Bsa Af593, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Thermo Fisher startingblock bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Startingblock Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher blocker bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Blocker Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 134 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Thermo Fisher bt bsa
    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a <t>FiTC-BSA</t> uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant
    Bt Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 76/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Thermo Fisher alexa bsa
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Alexa Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Thermo Fisher 680 bsa
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    680 Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 82/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher bsa dichlorodihydrofluorescein
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Bsa Dichlorodihydrofluorescein, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher bsa complex
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Bsa Complex, 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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    79
    Thermo Fisher bsa f5
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Bsa F5, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher ultrapure bsa
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Ultrapure Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 492 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher alexafluor488 bsa
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Alexafluor488 Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher klh bsa
    Analysis of symplastic and apoplastic accumulation of <t>Alexa-</t> <t>BSA</t> and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)
    Klh Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher bsa i
    Schematic representation of insertion site before and after heat shock induction leading to cisgenic line C44.4.146. Transgenes neomycin phosphotransferase II ( NptII ), D-amino acid oxidase 1 ( dao1 ) and flippase ( Flp ) are shown in red, genomic DNA of 'Golden Delicious' in yellow, regulatory elements in orange and FB <t>_MR5</t> and regulatory sequences in green. Vector sequences in the cisgenic line are colored black and flippase recognition target (FRT) and original border sites are indicated in purple. Circles with letters indicate the amplicons resulting by PCR with the corresponding primers. Amplification of B and C indicates presence of the excisable cassette, amplification of D the presence of the cisgene FB_MR5 . Amplicon E flanks the insertion site. F and G amplify the junction T- and genomic DNA at LB, and RB, respectively. In the structure of the insert in C44.4.146 both restriction sites <t>Bsa</t> I and Xba I, used for Southern blot analysis and iPCR, respectively, are indicated.
    Bsa I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Thermo Fisher alexa488 bsa
    Caveolin-1 RNAi reduced <t>Alexa488-BSA</t> endocytosis in pulmonary artery endothelial cells. ( A ) Representative immunoblot of cav-1 expression in RPAEC treated with transfection reagent only, sham siRNA, and cav-1 siRNA is shown with β-actin as loading control. Densitometric measurement was determined by NIH Image J software. Values are mean ± SEM. Significant difference from control (** P
    Alexa488 Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher bsa rpmi
    Caveolin-1 RNAi reduced <t>Alexa488-BSA</t> endocytosis in pulmonary artery endothelial cells. ( A ) Representative immunoblot of cav-1 expression in RPAEC treated with transfection reagent only, sham siRNA, and cav-1 siRNA is shown with β-actin as loading control. Densitometric measurement was determined by NIH Image J software. Values are mean ± SEM. Significant difference from control (** P
    Bsa Rpmi, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher bsa hi
    Modification of <t>HvCKX1</t> sequence induced by the KO-CKX1 construct in primary transgenic mutant plants. HvCKX1 sequence alignment of the nine mutants, where the mutation occurred in both alleles (A) ; six mutants, where the mutation occurred in one allele (B) and WT HvCKX1 sequence. Deduced amino acid sequences of the mutant proteins (C) . The red sequence represents the Cas9 target site and underlined italics sequence represents <t>Bsa</t> HI restriction site. The number of nucleotides deleted (dashed) or inserted (blue color) is shown to the right side of each sequence. The names of the lines are shown to left site of each sequence, where (a) and (b) of the lines 37, 39, 40, 43, 45, 49 represent two different sequences occurred. The red triangle indicates the DSB induction site.
    Bsa Hi, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher bsa buffer
    Modification of <t>HvCKX1</t> sequence induced by the KO-CKX1 construct in primary transgenic mutant plants. HvCKX1 sequence alignment of the nine mutants, where the mutation occurred in both alleles (A) ; six mutants, where the mutation occurred in one allele (B) and WT HvCKX1 sequence. Deduced amino acid sequences of the mutant proteins (C) . The red sequence represents the Cas9 target site and underlined italics sequence represents <t>Bsa</t> HI restriction site. The number of nucleotides deleted (dashed) or inserted (blue color) is shown to the right side of each sequence. The names of the lines are shown to left site of each sequence, where (a) and (b) of the lines 37, 39, 40, 43, 45, 49 represent two different sequences occurred. The red triangle indicates the DSB induction site.
    Bsa Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Thermo Fisher tmr bsa
    Inhibition of intracellular pH regulation, macropinocytosis, intracellular amino acid levels, and cell growth by a vacuolar (H + )‐ ATP ase (V‐ ATP ase) inhibitor. (a,b) Acridine Orange and AcidiFluor assays were undertaken in T‐24 bladder cancer cells 2 h after treatment with the indicated concentrations (Conc.) of bafilomycin A1 ( n = 4). Fluorescence (544/640 nm and 514/563 nm) was designated as the Y ‐axis. Data are presented as mean ± SD . (c) Macropinosome visualization was carried out with tetramethylrhodamine‐conjugated <t>BSA</t> ( <t>TMR</t> ‐ BSA ) for 30 min in T‐24 cells after 1 h pretreatment with 100 nM bafilomycin A1 (Baf) and 30 μM 5‐( N ‐ethyl‐ N ‐isopropyl) amiloride ( EIPA ). TMR dots (red) show levels of macropinocytosis. The macropinocytosis assay using TMR ‐ BSA was carried out in the same manner with the indicated concentrations of bafilomycin A1 or EIPA ( n = 4). TMR dots/cell are designated as the Y ‐axis. Data are presented as the mean ± SD . (d,e) T‐24 cells and HCT 116 colon cancer cells were treated with the indicated concentrations of bafilomycin A1. After 3 days, cell viability was assessed. Ordinate values were obtained by setting the control group value as 100%. Data are presented as mean ± SD ( n = 3). (f) Amino acid levels were analyzed in HCT 116 cells 8 h after treatment with 3 nM bafilomycin A1 using capillary electrophoresis time‐of‐flight mass spectrometry ( n = 3). Ordinate values were obtained by setting the control group value as 100% and designated as the Y ‐axis. Data are presented as mean ± SD . * P
    Tmr Bsa, supplied by Thermo Fisher, 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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    81
    Biosearch Technologies Inc np bsa
    Inhibition of intracellular pH regulation, macropinocytosis, intracellular amino acid levels, and cell growth by a vacuolar (H + )‐ ATP ase (V‐ ATP ase) inhibitor. (a,b) Acridine Orange and AcidiFluor assays were undertaken in T‐24 bladder cancer cells 2 h after treatment with the indicated concentrations (Conc.) of bafilomycin A1 ( n = 4). Fluorescence (544/640 nm and 514/563 nm) was designated as the Y ‐axis. Data are presented as mean ± SD . (c) Macropinosome visualization was carried out with tetramethylrhodamine‐conjugated <t>BSA</t> ( <t>TMR</t> ‐ BSA ) for 30 min in T‐24 cells after 1 h pretreatment with 100 nM bafilomycin A1 (Baf) and 30 μM 5‐( N ‐ethyl‐ N ‐isopropyl) amiloride ( EIPA ). TMR dots (red) show levels of macropinocytosis. The macropinocytosis assay using TMR ‐ BSA was carried out in the same manner with the indicated concentrations of bafilomycin A1 or EIPA ( n = 4). TMR dots/cell are designated as the Y ‐axis. Data are presented as the mean ± SD . (d,e) T‐24 cells and HCT 116 colon cancer cells were treated with the indicated concentrations of bafilomycin A1. After 3 days, cell viability was assessed. Ordinate values were obtained by setting the control group value as 100%. Data are presented as mean ± SD ( n = 3). (f) Amino acid levels were analyzed in HCT 116 cells 8 h after treatment with 3 nM bafilomycin A1 using capillary electrophoresis time‐of‐flight mass spectrometry ( n = 3). Ordinate values were obtained by setting the control group value as 100% and designated as the Y ‐axis. Data are presented as mean ± SD . * P
    Np Bsa, supplied by Biosearch Technologies Inc, used in various techniques. Bioz Stars score: 81/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher a647 bsa
    Actin binding mediated in part by MARCO scavenger receptor. Ex vivo wild-type (WT) and MARCO −/− BALF AMs were collected from lung lavage and preincubated (37°C, 40 min) with or without DS (100 μg/ml). AMs were washed and incubated in 20 μg/ml <t>A647-actin,</t> 20 μg/ml <t>A647-BSA,</t> or vehicle alone (4°C, 30 min) and washed in preparation for flow cytometry. A : mean fluorescence (FL) index (%parent × A647-fluorescence) observed via flow cytometry for WT, MARCO −/− (± DS) with A647-actin. B : mean FL index for WT, MARCO −/− (± DS) with A647-BSA. C : histograms for graph in A : WT, MARCO −/− (± DS) with A647-actin. Dark gray, WT + GAB; light gray, MARCO −/− + GAB; magenta, WT + actin, purple, WT + DS + actin; green, MARCO −/− + actin; red, MARCO −/− + DS + actin. D : histograms for graph in B : WT, MARCO −/− (± DS) with A647-BSA. Light gray, WT + BSA; green, WT + DS + BSA; purple, MARCO −/− + BSA; red, MARCO −/− + DS + BSA; magenta, WT + actin. All histograms represent A647-fluorescence intensity counts of 10,000 events/sample ( n = 3); * P
    A647 Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Comparison of in vitro experimental data with flow, fit to the diffusion-only and diffusion-convection models. A series of experimental fluorescence recovery curves for FITC-BSA and FITC-2000 kDa dextran were taken over a wide range of known flow

    Journal: Biophysical Journal

    Article Title: Improved Model of Fluorescence Recovery Expands the Application of Multiphoton Fluorescence Recovery after Photobleaching in Vivo

    doi: 10.1016/j.bpj.2009.04.020

    Figure Lengend Snippet: Comparison of in vitro experimental data with flow, fit to the diffusion-only and diffusion-convection models. A series of experimental fluorescence recovery curves for FITC-BSA and FITC-2000 kDa dextran were taken over a wide range of known flow

    Article Snippet: For in vitro testing of the flow model, fluorescent samples were produced by mixing fluorescein isothiocyanate (FITC) conjugated to bovine serum albumin (BSA) or 2000 kDa dextran (dextran) (Molecular Probes/Invitrogen) diluted to 1 mg/mL in phosphate buffered saline (PBS) with 1 μ L/mL red fluorescent microspheres (FluoSpheres; Molecular Probes/Invitrogen).

    Techniques: In Vitro, Flow Cytometry, Diffusion-based Assay, Convection, Fluorescence

    Results of fitting in vitro experimental data with flow to the diffusion-convection model. A series of experimental fluorescence recovery curves for FITC-BSA and FITC-2000 kDa dextran were taken over a wide range of known flow speeds (plotted

    Journal: Biophysical Journal

    Article Title: Improved Model of Fluorescence Recovery Expands the Application of Multiphoton Fluorescence Recovery after Photobleaching in Vivo

    doi: 10.1016/j.bpj.2009.04.020

    Figure Lengend Snippet: Results of fitting in vitro experimental data with flow to the diffusion-convection model. A series of experimental fluorescence recovery curves for FITC-BSA and FITC-2000 kDa dextran were taken over a wide range of known flow speeds (plotted

    Article Snippet: For in vitro testing of the flow model, fluorescent samples were produced by mixing fluorescein isothiocyanate (FITC) conjugated to bovine serum albumin (BSA) or 2000 kDa dextran (dextran) (Molecular Probes/Invitrogen) diluted to 1 mg/mL in phosphate buffered saline (PBS) with 1 μ L/mL red fluorescent microspheres (FluoSpheres; Molecular Probes/Invitrogen).

    Techniques: In Vitro, Flow Cytometry, Diffusion-based Assay, Convection, Fluorescence

    Deficiency of retromer causes reduced lysosomal activity. (A) HeLa and Vps35 KO cells were treated with AF647-conjugated BSA (200 µg/ml) in complete medium at 37°C for 1 h. Cells were then fixed and subjected to fluorescence microscopy. Graph represents the fluorescent intensity of endocytosed BSA conjugate within HeLa and Vps35 KO cells (means ± SEM). Two-tailed Student’s t test was used to determine the statistical significance ( n = 3). (B) HeLa, Vps35 KO, and Vps35-GFP rescue cells were treated with DQ-BSA Red (10 µg/ml) in complete medium at 37°C overnight. Cells were fixed and immunolabeled with antibodies against LAMP1, followed by Alexa Fluor–conjugated fluorescent secondary antibodies. Scale bars, 10 µm. Graph represents the fluorescent intensity of DQ-BSA Red within HeLa, Vps35 KO, and Vps35-GFP rescue cells (means ± SEM). Two-tailed Student’s t test was used to determine the statistical significance ( n = 3). *, P

    Journal: The Journal of Cell Biology

    Article Title: Retromer has a selective function in cargo sorting via endosome transport carriers

    doi: 10.1083/jcb.201806153

    Figure Lengend Snippet: Deficiency of retromer causes reduced lysosomal activity. (A) HeLa and Vps35 KO cells were treated with AF647-conjugated BSA (200 µg/ml) in complete medium at 37°C for 1 h. Cells were then fixed and subjected to fluorescence microscopy. Graph represents the fluorescent intensity of endocytosed BSA conjugate within HeLa and Vps35 KO cells (means ± SEM). Two-tailed Student’s t test was used to determine the statistical significance ( n = 3). (B) HeLa, Vps35 KO, and Vps35-GFP rescue cells were treated with DQ-BSA Red (10 µg/ml) in complete medium at 37°C overnight. Cells were fixed and immunolabeled with antibodies against LAMP1, followed by Alexa Fluor–conjugated fluorescent secondary antibodies. Scale bars, 10 µm. Graph represents the fluorescent intensity of DQ-BSA Red within HeLa, Vps35 KO, and Vps35-GFP rescue cells (means ± SEM). Two-tailed Student’s t test was used to determine the statistical significance ( n = 3). *, P

    Article Snippet: DQ Red BSA assay HeLa cells grown on coverslips were incubated with culture medium containing 10 µg/ml DQ Red BSA (Thermo Fisher Scientific) at 37°C overnight.

    Techniques: Activity Assay, Fluorescence, Microscopy, Two Tailed Test, Immunolabeling

    IαI and IαI domain HC2 can support attachment and survival of hPS cells. ( a ) Quantification of cell attachment by crystal violet staining 4 h after seeding of hiPS cell line K2C added to plates with 10 μg ml −1 VN-XF coating, 50 μg ml −1 IαI medium supplementation, 50 μg ml −1 HC1 coating or 50 μg ml −1 HC2 coating. ( b ) Immunofluorescence of hES cell line HUES1 on VN-XF coating or IαI supplement showing E-cadherin (left panel) and Oct4 (right panel), scale bar shows 100 μm. ( c ) Cell survival and growth assayed with crystal violet staining after 4 days of culture of HUES1 and K2C in E8 medium with IαI and different blocking antibodies, ( d ) E8 medium with or without 50 μg ml −1 IαI (E8:IαI), 5% BSA (w/v) in E8: IαI, and mTeSR1 medium with or without IαI; ( e ) E8 medium supplemented with IαI and IαI together with different integrin-blocking peptides. All cell-number quantification experiments were performed in triplicate over three separate experiments. Bars show mean±s.e.m. and statistical analysis over the three independent experiments. Statistical analysis indicates significant differences with * P

    Journal: Nature Communications

    Article Title: Human serum-derived protein removes the need for coating in defined human pluripotent stem cell culture

    doi: 10.1038/ncomms12170

    Figure Lengend Snippet: IαI and IαI domain HC2 can support attachment and survival of hPS cells. ( a ) Quantification of cell attachment by crystal violet staining 4 h after seeding of hiPS cell line K2C added to plates with 10 μg ml −1 VN-XF coating, 50 μg ml −1 IαI medium supplementation, 50 μg ml −1 HC1 coating or 50 μg ml −1 HC2 coating. ( b ) Immunofluorescence of hES cell line HUES1 on VN-XF coating or IαI supplement showing E-cadherin (left panel) and Oct4 (right panel), scale bar shows 100 μm. ( c ) Cell survival and growth assayed with crystal violet staining after 4 days of culture of HUES1 and K2C in E8 medium with IαI and different blocking antibodies, ( d ) E8 medium with or without 50 μg ml −1 IαI (E8:IαI), 5% BSA (w/v) in E8: IαI, and mTeSR1 medium with or without IαI; ( e ) E8 medium supplemented with IαI and IαI together with different integrin-blocking peptides. All cell-number quantification experiments were performed in triplicate over three separate experiments. Bars show mean±s.e.m. and statistical analysis over the three independent experiments. Statistical analysis indicates significant differences with * P

    Article Snippet: Other reagents: Hoechst 33342 (ThermoFisher), Matrigel™ Matrix hES-qualified (Corning), RGD-based blocking peptides (all from Bachem, described in ), Y-27632 (ROCK inhibitor, ROCKi, StemCell Technologies), 25% hES-qualified BSA (Invitrogen), high molecular weight HA 2,000–2,400 kDa (HMW-HA, Cat No. 73641, Sigma-Aldrich), and 4-Methylumbelliferone (4-MU, M1381, Sigma).

    Techniques: Cell Attachment Assay, Staining, Immunofluorescence, Blocking Assay

    GAL efficiently labels Gal and GalNAc residues on cell surface glycoproteins. ( A ) Asialo-K20 cells were incubated in PBS with 5 mg/mL BSA, pH 6.7, containing 250 μM aminooxy-biotin in the presence or absence of 10 mM aniline and 50 U/mL galactose

    Journal: Glycobiology

    Article Title: Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans

    doi: 10.1093/glycob/cws144

    Figure Lengend Snippet: GAL efficiently labels Gal and GalNAc residues on cell surface glycoproteins. ( A ) Asialo-K20 cells were incubated in PBS with 5 mg/mL BSA, pH 6.7, containing 250 μM aminooxy-biotin in the presence or absence of 10 mM aniline and 50 U/mL galactose

    Article Snippet: For the oxime ligation step, cells were suspended to 1 × 107 cells/mL in PBS/5% BSA, pH 6.7 containing 250 μM aminooxy-biotin, aminooxy-AF488 (Invitrogen Corporation) or aminooxy-FLAG peptide and 10 mM aniline (Sigma–Aldrich) for 90 min at 4°C with end-over-end mixing.

    Techniques: Incubation

    Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a FiTC-BSA uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant

    Journal: Nature Communications

    Article Title: Lysosomal protease deficiency or substrate overload induces an oxidative-stress mediated STAT3-dependent pathway of lysosomal homeostasis

    doi: 10.1038/s41467-018-07741-6

    Figure Lengend Snippet: Increased lysosomal proteolytic capacity induced by suppression of AEP activity. a FiTC-BSA uptake and DQ-BSA degradation rates in WT 3T3s treated (red circles) or untreated (blue squares) with 50 μM MVO26630 for 16 h. Data are means ± SEM of n = 8 microscopic fields for untreated and n = 15 microscopic fields for MVO-treated. (Scale bar = 20 μm). b Time course of degradation of oncostatin M receptor beta (Osmrβ) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by oncostatin M. Relative intensity of each Osmrβ band was calculated for three independent experiments. c Time course of degradation of epithelial growth factor receptor (EGFR) in WT MEFs treated (dashed grey line) or untreated (black solid line) with 50 μM MVO26630 for 16 h and AEP −/− MEFs (red solid line) following receptor downregulation by epithelial growth factor. Relative intensity of each EGFR band was calculated for three independent experiments. Statistical significance was calculated using a two-sided unpaired t- test. ns = not significant

    Article Snippet: WT 3T3 cells (5 × 104 cells) were grown on coverslips and treated with MVO 50 μM for 16 h. Then, cells were incubated with 10 μg/ml of DQ-BSA (Invitrogen) or 50 μg/ml of FiTC-BSA for 2 h at 37 °C, washed twice with PBS, then fixed with 4% paraformaldehyde in PBS for 20 min at room temperature, mounted using Vectashield mounting medium with DAPI (Vector Laboratories) and images were obtained using an LSM 700 confocal microscope (Carl Zeiss).

    Techniques: Activity Assay

    Analysis of symplastic and apoplastic accumulation of Alexa- BSA and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)

    Journal: Plant Signaling & Behavior

    Article Title: Comparative analysis of protein transport in the N. benthamiana vasculature reveals different destinations.

    doi: 10.4161/psb.6.11.17896

    Figure Lengend Snippet: Analysis of symplastic and apoplastic accumulation of Alexa- BSA and Alexa-Histone H1 in N. benthamiana leaf. (A, B) Confocal microscopic images of CF dye, Alexa-BSA and Alexa-Histone H1 in N. benthamiana petiole cross sections following application (A)

    Article Snippet: Alexa-BSA (66 kDa; Invitrogen) were diluted to 0.3mg/ml.

    Techniques:

    Leaf vascular pattern in L4 source/sink transition leaf following application of CF dye, Alexa -BSA or Alexa -Histone. Images were taken at 30 or 60 min following petiole or root application of fluorescent markers. Class II, III, IV, and V veins are identified

    Journal: Plant Signaling & Behavior

    Article Title: Comparative analysis of protein transport in the N. benthamiana vasculature reveals different destinations.

    doi: 10.4161/psb.6.11.17896

    Figure Lengend Snippet: Leaf vascular pattern in L4 source/sink transition leaf following application of CF dye, Alexa -BSA or Alexa -Histone. Images were taken at 30 or 60 min following petiole or root application of fluorescent markers. Class II, III, IV, and V veins are identified

    Article Snippet: Alexa-BSA (66 kDa; Invitrogen) were diluted to 0.3mg/ml.

    Techniques:

    Unloading pattern of CF dye (A-D), Alexa Fluor 488 BSA (E- H) and Alexa Fluor 488 Histone (I-L) in L5 sink leaf following L1 petiole application. Unloading pattern of CF dye (M-P), Alexa Fluor 488 BSA (Q-T) and Alexa Fluor 488 Histone (U-X) in L5 sink

    Journal: Plant Signaling & Behavior

    Article Title: Comparative analysis of protein transport in the N. benthamiana vasculature reveals different destinations.

    doi: 10.4161/psb.6.11.17896

    Figure Lengend Snippet: Unloading pattern of CF dye (A-D), Alexa Fluor 488 BSA (E- H) and Alexa Fluor 488 Histone (I-L) in L5 sink leaf following L1 petiole application. Unloading pattern of CF dye (M-P), Alexa Fluor 488 BSA (Q-T) and Alexa Fluor 488 Histone (U-X) in L5 sink

    Article Snippet: Alexa-BSA (66 kDa; Invitrogen) were diluted to 0.3mg/ml.

    Techniques:

    Schematic representation of insertion site before and after heat shock induction leading to cisgenic line C44.4.146. Transgenes neomycin phosphotransferase II ( NptII ), D-amino acid oxidase 1 ( dao1 ) and flippase ( Flp ) are shown in red, genomic DNA of 'Golden Delicious' in yellow, regulatory elements in orange and FB _MR5 and regulatory sequences in green. Vector sequences in the cisgenic line are colored black and flippase recognition target (FRT) and original border sites are indicated in purple. Circles with letters indicate the amplicons resulting by PCR with the corresponding primers. Amplification of B and C indicates presence of the excisable cassette, amplification of D the presence of the cisgene FB_MR5 . Amplicon E flanks the insertion site. F and G amplify the junction T- and genomic DNA at LB, and RB, respectively. In the structure of the insert in C44.4.146 both restriction sites Bsa I and Xba I, used for Southern blot analysis and iPCR, respectively, are indicated.

    Journal: PLoS ONE

    Article Title: Development of the First Cisgenic Apple with Increased Resistance to Fire Blight

    doi: 10.1371/journal.pone.0143980

    Figure Lengend Snippet: Schematic representation of insertion site before and after heat shock induction leading to cisgenic line C44.4.146. Transgenes neomycin phosphotransferase II ( NptII ), D-amino acid oxidase 1 ( dao1 ) and flippase ( Flp ) are shown in red, genomic DNA of 'Golden Delicious' in yellow, regulatory elements in orange and FB _MR5 and regulatory sequences in green. Vector sequences in the cisgenic line are colored black and flippase recognition target (FRT) and original border sites are indicated in purple. Circles with letters indicate the amplicons resulting by PCR with the corresponding primers. Amplification of B and C indicates presence of the excisable cassette, amplification of D the presence of the cisgene FB_MR5 . Amplicon E flanks the insertion site. F and G amplify the junction T- and genomic DNA at LB, and RB, respectively. In the structure of the insert in C44.4.146 both restriction sites Bsa I and Xba I, used for Southern blot analysis and iPCR, respectively, are indicated.

    Article Snippet: DNA (10 μg) from each line and plasmid p9-Dao-FLPi-FB_MR5 was digested with 100 units Bsa I (Thermo Fisher Scientific Inc. ©, Waltham, USA).

    Techniques: Plasmid Preparation, Polymerase Chain Reaction, Amplification, Southern Blot

    Caveolin-1 RNAi reduced Alexa488-BSA endocytosis in pulmonary artery endothelial cells. ( A ) Representative immunoblot of cav-1 expression in RPAEC treated with transfection reagent only, sham siRNA, and cav-1 siRNA is shown with β-actin as loading control. Densitometric measurement was determined by NIH Image J software. Values are mean ± SEM. Significant difference from control (** P

    Journal: PLoS ONE

    Article Title: Caveolae-Dependent and -Independent Uptake of Albumin in Cultured Rodent Pulmonary Endothelial Cells

    doi: 10.1371/journal.pone.0081903

    Figure Lengend Snippet: Caveolin-1 RNAi reduced Alexa488-BSA endocytosis in pulmonary artery endothelial cells. ( A ) Representative immunoblot of cav-1 expression in RPAEC treated with transfection reagent only, sham siRNA, and cav-1 siRNA is shown with β-actin as loading control. Densitometric measurement was determined by NIH Image J software. Values are mean ± SEM. Significant difference from control (** P

    Article Snippet: After serum starvation for 4 h, cells were incubated with 50 μg/ml of Alexa488-BSA (Life Technologies, Carlsbad, CA, USA) in HBSS for indicated time at 37°C.

    Techniques: Expressing, Transfection, Software

    Dynamic process of Alexa488-BSA endocytosis in cav-1 +/+ and cav-1 -/- MLEC. ( A ) Cav-1 +/+ and cav-1 -/- MLEC were serum starved for 4 h then incubated with Alexa488-BSA (50 µg/ml) in HBSS. Fluorescence signals were recorded from 0 min to 30 min under total internal reflection fluorescence (TIRF) microscopy. Images from indicated time points (1, 5, 10, 15 and 20 min) are shown. ( B ) Quantitative analyses of Alexa488-BSA uptake in cav-1 +/+ and cav-1 -/- MLEC were performed with MetaMorph software by measuring the fold change of fluorescence intensity compared to cav-1 +/+ MLEC at 1 min after treatment.

    Journal: PLoS ONE

    Article Title: Caveolae-Dependent and -Independent Uptake of Albumin in Cultured Rodent Pulmonary Endothelial Cells

    doi: 10.1371/journal.pone.0081903

    Figure Lengend Snippet: Dynamic process of Alexa488-BSA endocytosis in cav-1 +/+ and cav-1 -/- MLEC. ( A ) Cav-1 +/+ and cav-1 -/- MLEC were serum starved for 4 h then incubated with Alexa488-BSA (50 µg/ml) in HBSS. Fluorescence signals were recorded from 0 min to 30 min under total internal reflection fluorescence (TIRF) microscopy. Images from indicated time points (1, 5, 10, 15 and 20 min) are shown. ( B ) Quantitative analyses of Alexa488-BSA uptake in cav-1 +/+ and cav-1 -/- MLEC were performed with MetaMorph software by measuring the fold change of fluorescence intensity compared to cav-1 +/+ MLEC at 1 min after treatment.

    Article Snippet: After serum starvation for 4 h, cells were incubated with 50 μg/ml of Alexa488-BSA (Life Technologies, Carlsbad, CA, USA) in HBSS for indicated time at 37°C.

    Techniques: Incubation, Fluorescence, Microscopy, Software

    Albumin endocytosis is a competitive, temperature sensitive, and caveolae-associated process in pulmonary endothelial cells. ( A ) Time course of Alexa488-BSA endocytosis in rat pulmonary microvascular endothelial cells (RPMEC). Cells were serum starved and then incubated with Alexa488-BSA (50 µg/ml) for 0 to 30 min at 37°C. Images were taken by confocal microscopy (Olympus Fluoview 1000) at 60× (1.42 NA) magnification with 2X zoom. Representative fluorescence intensity analysis was determined by quantifying fluorescent intensity of 20-30 cells in 5 random fields using Imaris software. Values are mean ± SEM from 5 separate fields in each condition. Significant differences from control (*** P

    Journal: PLoS ONE

    Article Title: Caveolae-Dependent and -Independent Uptake of Albumin in Cultured Rodent Pulmonary Endothelial Cells

    doi: 10.1371/journal.pone.0081903

    Figure Lengend Snippet: Albumin endocytosis is a competitive, temperature sensitive, and caveolae-associated process in pulmonary endothelial cells. ( A ) Time course of Alexa488-BSA endocytosis in rat pulmonary microvascular endothelial cells (RPMEC). Cells were serum starved and then incubated with Alexa488-BSA (50 µg/ml) for 0 to 30 min at 37°C. Images were taken by confocal microscopy (Olympus Fluoview 1000) at 60× (1.42 NA) magnification with 2X zoom. Representative fluorescence intensity analysis was determined by quantifying fluorescent intensity of 20-30 cells in 5 random fields using Imaris software. Values are mean ± SEM from 5 separate fields in each condition. Significant differences from control (*** P

    Article Snippet: After serum starvation for 4 h, cells were incubated with 50 μg/ml of Alexa488-BSA (Life Technologies, Carlsbad, CA, USA) in HBSS for indicated time at 37°C.

    Techniques: Incubation, Confocal Microscopy, Fluorescence, Software

    Inhibition of macropinocytosis prevents Alexa488-BSA uptake by rat pulmonary endothelial cells. ( A ) RPMEC were serum starved for 4 h followed by pretreatment with various inhibitors of macropinocytosis for 30 min including amiloride (Na/H exchange inhibitor, 3 mM), Cytochalasin D (actin polymerization inhibitor, 10 µM), Gö6976 (PKC inhibitor, 10 µM), then cells were incubated with Alexa488-BSA (50 µg/ml) for 15 min and fixed with 2% paraformaldehyde for imaging. Images were taken by confocal microscopy (40× magnification). Representative images from three independent experiments are shown. ( B ) The fluorescence intensity was determined by Imaris software with data are present as mean ± SEM from three independent experiments. Significant differences from control (** P

    Journal: PLoS ONE

    Article Title: Caveolae-Dependent and -Independent Uptake of Albumin in Cultured Rodent Pulmonary Endothelial Cells

    doi: 10.1371/journal.pone.0081903

    Figure Lengend Snippet: Inhibition of macropinocytosis prevents Alexa488-BSA uptake by rat pulmonary endothelial cells. ( A ) RPMEC were serum starved for 4 h followed by pretreatment with various inhibitors of macropinocytosis for 30 min including amiloride (Na/H exchange inhibitor, 3 mM), Cytochalasin D (actin polymerization inhibitor, 10 µM), Gö6976 (PKC inhibitor, 10 µM), then cells were incubated with Alexa488-BSA (50 µg/ml) for 15 min and fixed with 2% paraformaldehyde for imaging. Images were taken by confocal microscopy (40× magnification). Representative images from three independent experiments are shown. ( B ) The fluorescence intensity was determined by Imaris software with data are present as mean ± SEM from three independent experiments. Significant differences from control (** P

    Article Snippet: After serum starvation for 4 h, cells were incubated with 50 μg/ml of Alexa488-BSA (Life Technologies, Carlsbad, CA, USA) in HBSS for indicated time at 37°C.

    Techniques: Inhibition, Incubation, Imaging, Confocal Microscopy, Fluorescence, Software

    Endocytosis of Alexa488-BSA occurs in cav-1 -/- MLEC through a caveolae-independent pathway. ( A ) Representative immunoblot of cav-1 expression in cav-1 +/+ and cav-1 -/- MLEC is shown with β-actin as loading control. ( B ) Fluorescent images and ( C ) confocal images of Alexa488-BSA (green) and cav-1 staining (red) in cav-1 +/+ and cav-1 -/- MLEC are shown (60× magnification). Cells were serum starved for 4 h and incubated with Alexa488-BSA (50 µg/ml) in HBSS for 30 min at 37°C, then cells were fixed and staining of cav-1 was performed. Representative images of three independent experiments are shown. ( D ) Fluorescence intensity analysis was determined by quantifying fluorescent intensity of 20-30 cells in 5 random fields with Imaris software. Values are mean ± SEM from two independent experiments.

    Journal: PLoS ONE

    Article Title: Caveolae-Dependent and -Independent Uptake of Albumin in Cultured Rodent Pulmonary Endothelial Cells

    doi: 10.1371/journal.pone.0081903

    Figure Lengend Snippet: Endocytosis of Alexa488-BSA occurs in cav-1 -/- MLEC through a caveolae-independent pathway. ( A ) Representative immunoblot of cav-1 expression in cav-1 +/+ and cav-1 -/- MLEC is shown with β-actin as loading control. ( B ) Fluorescent images and ( C ) confocal images of Alexa488-BSA (green) and cav-1 staining (red) in cav-1 +/+ and cav-1 -/- MLEC are shown (60× magnification). Cells were serum starved for 4 h and incubated with Alexa488-BSA (50 µg/ml) in HBSS for 30 min at 37°C, then cells were fixed and staining of cav-1 was performed. Representative images of three independent experiments are shown. ( D ) Fluorescence intensity analysis was determined by quantifying fluorescent intensity of 20-30 cells in 5 random fields with Imaris software. Values are mean ± SEM from two independent experiments.

    Article Snippet: After serum starvation for 4 h, cells were incubated with 50 μg/ml of Alexa488-BSA (Life Technologies, Carlsbad, CA, USA) in HBSS for indicated time at 37°C.

    Techniques: Expressing, Staining, Incubation, Fluorescence, Software

    Modification of HvCKX1 sequence induced by the KO-CKX1 construct in primary transgenic mutant plants. HvCKX1 sequence alignment of the nine mutants, where the mutation occurred in both alleles (A) ; six mutants, where the mutation occurred in one allele (B) and WT HvCKX1 sequence. Deduced amino acid sequences of the mutant proteins (C) . The red sequence represents the Cas9 target site and underlined italics sequence represents Bsa HI restriction site. The number of nucleotides deleted (dashed) or inserted (blue color) is shown to the right side of each sequence. The names of the lines are shown to left site of each sequence, where (a) and (b) of the lines 37, 39, 40, 43, 45, 49 represent two different sequences occurred. The red triangle indicates the DSB induction site.

    Journal: Frontiers in Plant Science

    Article Title: Modification of Barley Plant Productivity Through Regulation of Cytokinin Content by Reverse-Genetics Approaches

    doi: 10.3389/fpls.2018.01676

    Figure Lengend Snippet: Modification of HvCKX1 sequence induced by the KO-CKX1 construct in primary transgenic mutant plants. HvCKX1 sequence alignment of the nine mutants, where the mutation occurred in both alleles (A) ; six mutants, where the mutation occurred in one allele (B) and WT HvCKX1 sequence. Deduced amino acid sequences of the mutant proteins (C) . The red sequence represents the Cas9 target site and underlined italics sequence represents Bsa HI restriction site. The number of nucleotides deleted (dashed) or inserted (blue color) is shown to the right side of each sequence. The names of the lines are shown to left site of each sequence, where (a) and (b) of the lines 37, 39, 40, 43, 45, 49 represent two different sequences occurred. The red triangle indicates the DSB induction site.

    Article Snippet: The 756 bp PCR product, covering part of the first HvCKX1 exon, was digested with Bsa HI (Thermo Fischer Scientific, Waltham, MA, United States).

    Techniques: Modification, Sequencing, Construct, Transgenic Assay, Mutagenesis

    Inhibition of intracellular pH regulation, macropinocytosis, intracellular amino acid levels, and cell growth by a vacuolar (H + )‐ ATP ase (V‐ ATP ase) inhibitor. (a,b) Acridine Orange and AcidiFluor assays were undertaken in T‐24 bladder cancer cells 2 h after treatment with the indicated concentrations (Conc.) of bafilomycin A1 ( n = 4). Fluorescence (544/640 nm and 514/563 nm) was designated as the Y ‐axis. Data are presented as mean ± SD . (c) Macropinosome visualization was carried out with tetramethylrhodamine‐conjugated BSA ( TMR ‐ BSA ) for 30 min in T‐24 cells after 1 h pretreatment with 100 nM bafilomycin A1 (Baf) and 30 μM 5‐( N ‐ethyl‐ N ‐isopropyl) amiloride ( EIPA ). TMR dots (red) show levels of macropinocytosis. The macropinocytosis assay using TMR ‐ BSA was carried out in the same manner with the indicated concentrations of bafilomycin A1 or EIPA ( n = 4). TMR dots/cell are designated as the Y ‐axis. Data are presented as the mean ± SD . (d,e) T‐24 cells and HCT 116 colon cancer cells were treated with the indicated concentrations of bafilomycin A1. After 3 days, cell viability was assessed. Ordinate values were obtained by setting the control group value as 100%. Data are presented as mean ± SD ( n = 3). (f) Amino acid levels were analyzed in HCT 116 cells 8 h after treatment with 3 nM bafilomycin A1 using capillary electrophoresis time‐of‐flight mass spectrometry ( n = 3). Ordinate values were obtained by setting the control group value as 100% and designated as the Y ‐axis. Data are presented as mean ± SD . * P

    Journal: Cancer Science

    Article Title: Cancer with low cathepsin D levels is susceptible to vacuolar (H+)‐ATPase inhibition

    doi: 10.1111/cas.13240

    Figure Lengend Snippet: Inhibition of intracellular pH regulation, macropinocytosis, intracellular amino acid levels, and cell growth by a vacuolar (H + )‐ ATP ase (V‐ ATP ase) inhibitor. (a,b) Acridine Orange and AcidiFluor assays were undertaken in T‐24 bladder cancer cells 2 h after treatment with the indicated concentrations (Conc.) of bafilomycin A1 ( n = 4). Fluorescence (544/640 nm and 514/563 nm) was designated as the Y ‐axis. Data are presented as mean ± SD . (c) Macropinosome visualization was carried out with tetramethylrhodamine‐conjugated BSA ( TMR ‐ BSA ) for 30 min in T‐24 cells after 1 h pretreatment with 100 nM bafilomycin A1 (Baf) and 30 μM 5‐( N ‐ethyl‐ N ‐isopropyl) amiloride ( EIPA ). TMR dots (red) show levels of macropinocytosis. The macropinocytosis assay using TMR ‐ BSA was carried out in the same manner with the indicated concentrations of bafilomycin A1 or EIPA ( n = 4). TMR dots/cell are designated as the Y ‐axis. Data are presented as the mean ± SD . (d,e) T‐24 cells and HCT 116 colon cancer cells were treated with the indicated concentrations of bafilomycin A1. After 3 days, cell viability was assessed. Ordinate values were obtained by setting the control group value as 100%. Data are presented as mean ± SD ( n = 3). (f) Amino acid levels were analyzed in HCT 116 cells 8 h after treatment with 3 nM bafilomycin A1 using capillary electrophoresis time‐of‐flight mass spectrometry ( n = 3). Ordinate values were obtained by setting the control group value as 100% and designated as the Y ‐axis. Data are presented as mean ± SD . * P

    Article Snippet: After 1 h, 0.4 mg/mL TMR‐BSA (Life Technologies, Carlsbad, CA, USA) was added to the wells, and cells were incubated for 30 min.

    Techniques: Inhibition, Fluorescence, Electrophoresis, Mass Spectrometry

    Actin binding mediated in part by MARCO scavenger receptor. Ex vivo wild-type (WT) and MARCO −/− BALF AMs were collected from lung lavage and preincubated (37°C, 40 min) with or without DS (100 μg/ml). AMs were washed and incubated in 20 μg/ml A647-actin, 20 μg/ml A647-BSA, or vehicle alone (4°C, 30 min) and washed in preparation for flow cytometry. A : mean fluorescence (FL) index (%parent × A647-fluorescence) observed via flow cytometry for WT, MARCO −/− (± DS) with A647-actin. B : mean FL index for WT, MARCO −/− (± DS) with A647-BSA. C : histograms for graph in A : WT, MARCO −/− (± DS) with A647-actin. Dark gray, WT + GAB; light gray, MARCO −/− + GAB; magenta, WT + actin, purple, WT + DS + actin; green, MARCO −/− + actin; red, MARCO −/− + DS + actin. D : histograms for graph in B : WT, MARCO −/− (± DS) with A647-BSA. Light gray, WT + BSA; green, WT + DS + BSA; purple, MARCO −/− + BSA; red, MARCO −/− + DS + BSA; magenta, WT + actin. All histograms represent A647-fluorescence intensity counts of 10,000 events/sample ( n = 3); * P

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    Article Title: Free actin impairs macrophage bacterial defenses via scavenger receptor MARCO interaction with reversal by plasma gelsolin

    doi: 10.1152/ajplung.00067.2017

    Figure Lengend Snippet: Actin binding mediated in part by MARCO scavenger receptor. Ex vivo wild-type (WT) and MARCO −/− BALF AMs were collected from lung lavage and preincubated (37°C, 40 min) with or without DS (100 μg/ml). AMs were washed and incubated in 20 μg/ml A647-actin, 20 μg/ml A647-BSA, or vehicle alone (4°C, 30 min) and washed in preparation for flow cytometry. A : mean fluorescence (FL) index (%parent × A647-fluorescence) observed via flow cytometry for WT, MARCO −/− (± DS) with A647-actin. B : mean FL index for WT, MARCO −/− (± DS) with A647-BSA. C : histograms for graph in A : WT, MARCO −/− (± DS) with A647-actin. Dark gray, WT + GAB; light gray, MARCO −/− + GAB; magenta, WT + actin, purple, WT + DS + actin; green, MARCO −/− + actin; red, MARCO −/− + DS + actin. D : histograms for graph in B : WT, MARCO −/− (± DS) with A647-BSA. Light gray, WT + BSA; green, WT + DS + BSA; purple, MARCO −/− + BSA; red, MARCO −/− + DS + BSA; magenta, WT + actin. All histograms represent A647-fluorescence intensity counts of 10,000 events/sample ( n = 3); * P

    Article Snippet: Remaining cells were washed twice in DPBS, and all cells were exposed to 40 μg/ml A647-actin, 40 μg/ml A647-BSA (Molecular Probes, Thermo Fisher Scientific), or vehicle alone (GAB, 50% RPMI 1640, 0.5% BSA) while protected from light at 4°C for 30 min.

    Techniques: Binding Assay, Ex Vivo, Affinity Magnetic Separation, Incubation, Flow Cytometry, Cytometry, Fluorescence

    Free actin binds human alveolar macrophages in vitro in a scavenger receptor (SR)-dependent fashion. Scanning cytometry fluorescence imaging. Human GM-Mϕs were incubated (37°C, 40 min) with or without the pan-SR inhibitor PolyI (25 μg/ml), washed in Dulbecco’s phosphate-buffered saline (DPBS), and exposed to 40 μg/ml Alexa Fluor 647-conjugated actin from rabbit skeletal muscle, 40 μg/ml Alexa Fluor 647-conjugated albumin from bovine serum albumin (BSA), or vehicle alone (4°C, 30 min). Cells were labeled with Hoechst and Cell Mask Blue. Representative images are collapsed confocal stacked images. A–E : cells incubated with A647-actin ( n = 5 experiments, 15 wells total; A ), A647-actin with PolyI ( n = 2 experiments, 6 wells total; B ), vehicle control ( n = 5 experiments, 15 wells total; C ), A647-BSA ( n = 5 experiments, 15 wells total; D ), or A647-BSA with PolyI ( n = 2 experiments, 6 wells total; E ). F : value of A647 fluorescence for total cell cytoplasm above baseline staining for all cells, showing increased binding of actin by human GM-Mϕs compared with equivalent concentrations of control protein albumin. Actin binding is significantly reduced in the presence of pan-SR inhibitors. Data are mean fluorescence (FL) ± SE; **** P = 0.0001; ●, ■, ▲, ◆, gray circles, and gray squares all correspond to samples from groups defined in the x -axis.

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    Article Title: Free actin impairs macrophage bacterial defenses via scavenger receptor MARCO interaction with reversal by plasma gelsolin

    doi: 10.1152/ajplung.00067.2017

    Figure Lengend Snippet: Free actin binds human alveolar macrophages in vitro in a scavenger receptor (SR)-dependent fashion. Scanning cytometry fluorescence imaging. Human GM-Mϕs were incubated (37°C, 40 min) with or without the pan-SR inhibitor PolyI (25 μg/ml), washed in Dulbecco’s phosphate-buffered saline (DPBS), and exposed to 40 μg/ml Alexa Fluor 647-conjugated actin from rabbit skeletal muscle, 40 μg/ml Alexa Fluor 647-conjugated albumin from bovine serum albumin (BSA), or vehicle alone (4°C, 30 min). Cells were labeled with Hoechst and Cell Mask Blue. Representative images are collapsed confocal stacked images. A–E : cells incubated with A647-actin ( n = 5 experiments, 15 wells total; A ), A647-actin with PolyI ( n = 2 experiments, 6 wells total; B ), vehicle control ( n = 5 experiments, 15 wells total; C ), A647-BSA ( n = 5 experiments, 15 wells total; D ), or A647-BSA with PolyI ( n = 2 experiments, 6 wells total; E ). F : value of A647 fluorescence for total cell cytoplasm above baseline staining for all cells, showing increased binding of actin by human GM-Mϕs compared with equivalent concentrations of control protein albumin. Actin binding is significantly reduced in the presence of pan-SR inhibitors. Data are mean fluorescence (FL) ± SE; **** P = 0.0001; ●, ■, ▲, ◆, gray circles, and gray squares all correspond to samples from groups defined in the x -axis.

    Article Snippet: Remaining cells were washed twice in DPBS, and all cells were exposed to 40 μg/ml A647-actin, 40 μg/ml A647-BSA (Molecular Probes, Thermo Fisher Scientific), or vehicle alone (GAB, 50% RPMI 1640, 0.5% BSA) while protected from light at 4°C for 30 min.

    Techniques: In Vitro, Cytometry, Fluorescence, Imaging, Incubation, Labeling, Staining, Binding Assay