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  • 99
    Thermo Fisher bovine serum albumine bsa
    Probe development and preliminary characterization. ( a ) Schematic of modular smFP construction. sfGFP shown in cartoon; chromophore either left intact or rendered invisible (grey). Epitope tags are inserted at the N- (Ins 1, blue sphere) and C- (Ins 3, red) termini and into a loop (Ins 2, yellow). ( b–c ) Fluorescence correlation spectroscopy (FCS) measurements to quantify antibody binding to FLAG epitopes of smFP, based on changes in diffusion with molecular weight. ( b ) Calibration of solution-phase diffusion time τ D and diffusion coefficient D versus molecular weight (MW) measured by FCS. Molecular weight markers were: hydrolyzed <t>Alexa488,</t> 534 Da; hydrolyzed Alexa546, 963 Da; epidermal growth factor (EGF)-FITC, 6.5 kDa; EGFP, 32.7 kDa; smFP_FLAG_bright, 42.3 kDa; bovine serum albumin <t>(BSA)-Alexa488,</t> 69 kDa; anti-FLAG M2-FITC, 153 kDa. n = 5 experimental replicates; mean ± SD shown. Data was fit to a power-law: τ D = (0.072 ± 0.006) ×MW (0.39±0.02) (± SEM, R 2 = 0.99). Diffusion time and diffusion coefficient are related by D = w o 2 /8 τ D , where w o is the e −2 laser-beam radius, here w o = 430 nm at 940 nm excitation. Also shown are literature values of diffusion coefficients of proteins 47 , and dyes and proteins measured using scanning FCS 48 . c ) FCS-determined diffusion times of 10 nM smFP_FLAG_bright (with 10 FLAG copies per protein yielding 100 nM of FLAG epitopes) titrated with monoclonal antibodies against GFP (Invitrogen rabbit monoclonal) or FLAG (Sigma M2), which shows saturated binding above 100 nM antibody; and 10 nM smFP_3xFLAG_bright (30 nM epitopes) with anti-FLAG antibody, which shows saturated binding above 30 nM antibody. n = 5 experimental replicates for titrations; mean ± SD shown. Ladder at right is the calculated number of antibodies bound to smFP (42.3 kDa) for the corresponding τ D , based on the calibration obtained in c ). d ) Fly brains showing expression and staining of smFP probes. R59A05-GAL4 49 crossed with UAS-myr-smFP flies, with myr-sfGFP as a control. All probes, including sfGFP, lack chromophores. Dissected fly brains were stained with anti-tag antibodies or anti-GFP and Alexa488-conjugated secondaries, in small volumes (~10 µl); slight differences in staining are likely due to variation in antibody penetration. Scale bar, 50 µm.
    Bovine Serum Albumine Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2529 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam bovine serum albumen bsa
    NF B cells express <t>laminin</t> α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface integrin expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or <t>BSA.</t> Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), α6 (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P
    Bovine Serum Albumen Bsa, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 969 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher bovine serum albumin bsa
    Determination of <t>NBD</t> C6-Cer glycosylation in cells. NCI/ADR-RES cells cultured for 24 hr were switched to 1% <t>BSA</t> RPMI-1640 medium containing NBD C6-Cer for enzymatic reactions. ( a ) Fluorescent NBD-sphingolipids in cells after incubations with 2 µM NBD C6-Cer. Green, NBD-sphingolipids; Blue, DAPI-nuclei. Images (200× magnification) were captured using an EVOS FL cell imaging system. ( b ) Dose-response for Cer glycosylation by GCS. Cells were incubated with NBD C6-Cer for 2 h. The correlation coefficient for cellular C6-Cer (dashed line) to NBD C6-Cer in medium is 0.91, and for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. ( c ) Time course of cellular Cer glycosylation. Cells were incubated with 2.0 µM of NBD C6-Cer for indicated periods. The correlation coefficient for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. Results represent the mean ± SD of three independent enzyme reactions.
    Bovine Serum Albumin Bsa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9418 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Tocris bovine serum albumin bsa
    Verification of common genes according to GO analysis by real-time PCR. A: Genes up-regulated by NMDA and down-regulated by MK801; B: Genes down-regulated by NMDA and up-regulated by MK801. Primary calvarial osteoblasts were cultured in medium with 0.2% <t>BSA</t> containing 0.5 mmol/L NMDA or 100 μmol/L MK801 for 48 h. mRNAs were isolated after 48 h and subjected to quantitative real-time PCR with primers described in Table 1 . Comparative threshold values represent the mean of three samples normalized to GAPDH levels. Values are relative to those obtained from the vehicle groups. b P
    Bovine Serum Albumin Bsa, supplied by Tocris, used in various techniques. Bioz Stars score: 94/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 22 article reviews
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    Image Search Results


    Probe development and preliminary characterization. ( a ) Schematic of modular smFP construction. sfGFP shown in cartoon; chromophore either left intact or rendered invisible (grey). Epitope tags are inserted at the N- (Ins 1, blue sphere) and C- (Ins 3, red) termini and into a loop (Ins 2, yellow). ( b–c ) Fluorescence correlation spectroscopy (FCS) measurements to quantify antibody binding to FLAG epitopes of smFP, based on changes in diffusion with molecular weight. ( b ) Calibration of solution-phase diffusion time τ D and diffusion coefficient D versus molecular weight (MW) measured by FCS. Molecular weight markers were: hydrolyzed Alexa488, 534 Da; hydrolyzed Alexa546, 963 Da; epidermal growth factor (EGF)-FITC, 6.5 kDa; EGFP, 32.7 kDa; smFP_FLAG_bright, 42.3 kDa; bovine serum albumin (BSA)-Alexa488, 69 kDa; anti-FLAG M2-FITC, 153 kDa. n = 5 experimental replicates; mean ± SD shown. Data was fit to a power-law: τ D = (0.072 ± 0.006) ×MW (0.39±0.02) (± SEM, R 2 = 0.99). Diffusion time and diffusion coefficient are related by D = w o 2 /8 τ D , where w o is the e −2 laser-beam radius, here w o = 430 nm at 940 nm excitation. Also shown are literature values of diffusion coefficients of proteins 47 , and dyes and proteins measured using scanning FCS 48 . c ) FCS-determined diffusion times of 10 nM smFP_FLAG_bright (with 10 FLAG copies per protein yielding 100 nM of FLAG epitopes) titrated with monoclonal antibodies against GFP (Invitrogen rabbit monoclonal) or FLAG (Sigma M2), which shows saturated binding above 100 nM antibody; and 10 nM smFP_3xFLAG_bright (30 nM epitopes) with anti-FLAG antibody, which shows saturated binding above 30 nM antibody. n = 5 experimental replicates for titrations; mean ± SD shown. Ladder at right is the calculated number of antibodies bound to smFP (42.3 kDa) for the corresponding τ D , based on the calibration obtained in c ). d ) Fly brains showing expression and staining of smFP probes. R59A05-GAL4 49 crossed with UAS-myr-smFP flies, with myr-sfGFP as a control. All probes, including sfGFP, lack chromophores. Dissected fly brains were stained with anti-tag antibodies or anti-GFP and Alexa488-conjugated secondaries, in small volumes (~10 µl); slight differences in staining are likely due to variation in antibody penetration. Scale bar, 50 µm.

    Journal: Nature methods

    Article Title: High-performance probes for light and electron microscopy

    doi: 10.1038/nmeth.3365

    Figure Lengend Snippet: Probe development and preliminary characterization. ( a ) Schematic of modular smFP construction. sfGFP shown in cartoon; chromophore either left intact or rendered invisible (grey). Epitope tags are inserted at the N- (Ins 1, blue sphere) and C- (Ins 3, red) termini and into a loop (Ins 2, yellow). ( b–c ) Fluorescence correlation spectroscopy (FCS) measurements to quantify antibody binding to FLAG epitopes of smFP, based on changes in diffusion with molecular weight. ( b ) Calibration of solution-phase diffusion time τ D and diffusion coefficient D versus molecular weight (MW) measured by FCS. Molecular weight markers were: hydrolyzed Alexa488, 534 Da; hydrolyzed Alexa546, 963 Da; epidermal growth factor (EGF)-FITC, 6.5 kDa; EGFP, 32.7 kDa; smFP_FLAG_bright, 42.3 kDa; bovine serum albumin (BSA)-Alexa488, 69 kDa; anti-FLAG M2-FITC, 153 kDa. n = 5 experimental replicates; mean ± SD shown. Data was fit to a power-law: τ D = (0.072 ± 0.006) ×MW (0.39±0.02) (± SEM, R 2 = 0.99). Diffusion time and diffusion coefficient are related by D = w o 2 /8 τ D , where w o is the e −2 laser-beam radius, here w o = 430 nm at 940 nm excitation. Also shown are literature values of diffusion coefficients of proteins 47 , and dyes and proteins measured using scanning FCS 48 . c ) FCS-determined diffusion times of 10 nM smFP_FLAG_bright (with 10 FLAG copies per protein yielding 100 nM of FLAG epitopes) titrated with monoclonal antibodies against GFP (Invitrogen rabbit monoclonal) or FLAG (Sigma M2), which shows saturated binding above 100 nM antibody; and 10 nM smFP_3xFLAG_bright (30 nM epitopes) with anti-FLAG antibody, which shows saturated binding above 30 nM antibody. n = 5 experimental replicates for titrations; mean ± SD shown. Ladder at right is the calculated number of antibodies bound to smFP (42.3 kDa) for the corresponding τ D , based on the calibration obtained in c ). d ) Fly brains showing expression and staining of smFP probes. R59A05-GAL4 49 crossed with UAS-myr-smFP flies, with myr-sfGFP as a control. All probes, including sfGFP, lack chromophores. Dissected fly brains were stained with anti-tag antibodies or anti-GFP and Alexa488-conjugated secondaries, in small volumes (~10 µl); slight differences in staining are likely due to variation in antibody penetration. Scale bar, 50 µm.

    Article Snippet: Calibration of diffusion time versus molecular weight was obtained using the following markers: hydrolyzed Alexa488, 534 Da (A-20000, Invitrogen); hydrolyzed Alexa546, 963 Da (A-20002, Invitrogen); epidermal growth factor (EGF)-FITC, 6.5 kDa (E-3478, Invitrogen); EGFP, 32.7 kDa (4999-100 Biovision); RSET-smFP_FLAG_bright, 42.3 kDa; bovine serum albumin (BSA)-Alexa488, 69 kDa (A13100, Invitrogen); M2 anti-FLAG mAb-FITC, 153 kDa.

    Techniques: Fluorescence, Spectroscopy, Binding Assay, Diffusion-based Assay, Molecular Weight, Expressing, Staining

    QuaMeter generates metrics similar to MSQC with the exception of chromatographic metrics due to the use of distinct chromatogram extraction tools. Metrics were generated from BSA QC experiments collected on a Thermo Fisher LTQ-XL mass spectrometer. The

    Journal: Analytical chemistry

    Article Title: QuaMeter: Multivendor Performance Metrics for LC-MS/MS Proteomics Instrumentation

    doi: 10.1021/ac300629p

    Figure Lengend Snippet: QuaMeter generates metrics similar to MSQC with the exception of chromatographic metrics due to the use of distinct chromatogram extraction tools. Metrics were generated from BSA QC experiments collected on a Thermo Fisher LTQ-XL mass spectrometer. The

    Article Snippet: Data from bovine serum albumin (BSA) QC samples analyzed on a Thermo Fisher LTQ-XL mass spectrometer were employed to evaluate how code differences altered values reported by these two tools.

    Techniques: Generated, Mass Spectrometry

    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface integrin expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), α6 (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P

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

    Article Title: Extracellular matrix of secondary lymphoid organs impacts on B-cell fate and survival

    doi: 10.1073/pnas.1218131110

    Figure Lengend Snippet: NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface integrin expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), α6 (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P

    Article Snippet: Ninety-six-well ELISA plates were coated overnight at 4 °C with BSA, agrin, laminin 411, laminin 511, or fibronectin (3 µg/mL) and blocked with 2% (wt/vol) BSA, and BAFF (R & D 500 ng/mL) was added at room temperature for 2 h. Rat anti-BAFF (Abcam, 1 µg/mL) and HRP-conjugated goat anti-rat were used to detect bound BAFF.

    Techniques: Binding Assay, Flow Cytometry, Cytometry, Expressing, In Vitro, Blocking Assay, Immunofluorescence, Staining, Mouse Assay, In Vivo, Ex Vivo, Labeling, Isolation, Injection

    Determination of NBD C6-Cer glycosylation in cells. NCI/ADR-RES cells cultured for 24 hr were switched to 1% BSA RPMI-1640 medium containing NBD C6-Cer for enzymatic reactions. ( a ) Fluorescent NBD-sphingolipids in cells after incubations with 2 µM NBD C6-Cer. Green, NBD-sphingolipids; Blue, DAPI-nuclei. Images (200× magnification) were captured using an EVOS FL cell imaging system. ( b ) Dose-response for Cer glycosylation by GCS. Cells were incubated with NBD C6-Cer for 2 h. The correlation coefficient for cellular C6-Cer (dashed line) to NBD C6-Cer in medium is 0.91, and for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. ( c ) Time course of cellular Cer glycosylation. Cells were incubated with 2.0 µM of NBD C6-Cer for indicated periods. The correlation coefficient for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. Results represent the mean ± SD of three independent enzyme reactions.

    Journal: Scientific Reports

    Article Title: Incorporation of Fluorescence Ceramide-Based HPLC Assay for Rapidly and Efficiently Assessing Glucosylceramide Synthase In Vivo

    doi: 10.1038/s41598-017-03320-9

    Figure Lengend Snippet: Determination of NBD C6-Cer glycosylation in cells. NCI/ADR-RES cells cultured for 24 hr were switched to 1% BSA RPMI-1640 medium containing NBD C6-Cer for enzymatic reactions. ( a ) Fluorescent NBD-sphingolipids in cells after incubations with 2 µM NBD C6-Cer. Green, NBD-sphingolipids; Blue, DAPI-nuclei. Images (200× magnification) were captured using an EVOS FL cell imaging system. ( b ) Dose-response for Cer glycosylation by GCS. Cells were incubated with NBD C6-Cer for 2 h. The correlation coefficient for cellular C6-Cer (dashed line) to NBD C6-Cer in medium is 0.91, and for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. ( c ) Time course of cellular Cer glycosylation. Cells were incubated with 2.0 µM of NBD C6-Cer for indicated periods. The correlation coefficient for cellular C6-GlcCer (solid line) to NBD C6-Cer in medium is 0.99. Results represent the mean ± SD of three independent enzyme reactions.

    Article Snippet: Materials N -[6-[(7-nitro-2,1,3-benzoxadiazol-4-yl) amino]hexanoyl]-d -erythro -sphingosine (NBD C6-ceramide), as well as NBD C6-Cer complexed to bovine serum albumin (BSA) (1:4, w/w), were purchased from Invitrogen (Carlsbad, CA).

    Techniques: Cell Culture, Imaging, Incubation

    Verification of common genes according to GO analysis by real-time PCR. A: Genes up-regulated by NMDA and down-regulated by MK801; B: Genes down-regulated by NMDA and up-regulated by MK801. Primary calvarial osteoblasts were cultured in medium with 0.2% BSA containing 0.5 mmol/L NMDA or 100 μmol/L MK801 for 48 h. mRNAs were isolated after 48 h and subjected to quantitative real-time PCR with primers described in Table 1 . Comparative threshold values represent the mean of three samples normalized to GAPDH levels. Values are relative to those obtained from the vehicle groups. b P

    Journal: Acta Pharmacologica Sinica

    Article Title: Multiple signaling pathways involved in stimulation of osteoblast differentiation by N-methyl-D-aspartate receptors activation in vitro

    doi: 10.1038/aps.2011.38

    Figure Lengend Snippet: Verification of common genes according to GO analysis by real-time PCR. A: Genes up-regulated by NMDA and down-regulated by MK801; B: Genes down-regulated by NMDA and up-regulated by MK801. Primary calvarial osteoblasts were cultured in medium with 0.2% BSA containing 0.5 mmol/L NMDA or 100 μmol/L MK801 for 48 h. mRNAs were isolated after 48 h and subjected to quantitative real-time PCR with primers described in Table 1 . Comparative threshold values represent the mean of three samples normalized to GAPDH levels. Values are relative to those obtained from the vehicle groups. b P

    Article Snippet: After 4 d of culture, cells were starved with serum-free α-MEM and 0.2% bovine serum albumin (BSA) for 12 h. Cultures were also exposed to fresh serum-free medium with 0.2% BSA with or without NMDA, MK801 (both from Tocris Cookson Ltd UK), or other inhibitors.

    Techniques: Real-time Polymerase Chain Reaction, Cell Culture, Isolation