biotinylated fragments Search Results


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  • 95
    Millipore biotinylated hyaluronan proteoglycan fragment
    Biotinylated Hyaluronan Proteoglycan Fragment, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Seikagaku biotinylated fragment
    Biotinylated Fragment, supplied by Seikagaku, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Thermo Fisher biotinylated fragments
    Biotinylated Fragments, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 301 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies biotinylated fragment
    Biotinylated Fragment, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    GE Healthcare biotinylated fragments
    Biotinylated Fragments, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    TaKaRa biotinylated hs fragments b hs
    Biotinylated Hs Fragments B Hs, supplied by TaKaRa, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher fragmented biotinylated crnas
    Fragmented Biotinylated Crnas, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Jackson Immuno mono biotinylated fragment
    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with <t>mono-biotinylated</t> fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p
    Mono Biotinylated Fragment, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Horizon Discovery biotinylated 5 end rna fragments
    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with <t>mono-biotinylated</t> fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p
    Biotinylated 5 End Rna Fragments, supplied by Horizon Discovery, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Nugen biotinylated
    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with <t>mono-biotinylated</t> fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p
    Biotinylated, supplied by Nugen, used in various techniques. Bioz Stars score: 92/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno biotinylated fab fragment
    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with <t>mono-biotinylated</t> fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p
    Biotinylated Fab Fragment, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher biotinylated rna fragments
    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with <t>mono-biotinylated</t> fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p
    Biotinylated Rna Fragments, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher biotinylated dna fragments
    ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic <t>DNA</t> (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a <t>biotinylated</t> Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).
    Biotinylated Dna Fragments, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 321 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies biotinylated
    ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic <t>DNA</t> (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a <t>biotinylated</t> Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).
    Biotinylated, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Abcam biotinylated fab fragments
    ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic <t>DNA</t> (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a <t>biotinylated</t> Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).
    Biotinylated Fab Fragments, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Jackson Immuno biotinylated fab fragment secondary antibodies
    ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic <t>DNA</t> (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a <t>biotinylated</t> Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).
    Biotinylated Fab Fragment Secondary Antibodies, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    AnaSpec biotinylated aβ fragments 1
    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the <t>Aβ-fibrinogen</t> interaction. (A) <t>Biotinylated</t> Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated
    Biotinylated Aβ Fragments 1, supplied by AnaSpec, 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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    Jackson Immuno biotinylated anti mouse fab fragments
    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the <t>Aβ-fibrinogen</t> interaction. (A) <t>Biotinylated</t> Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated
    Biotinylated Anti Mouse Fab Fragments, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The Jackson Laboratory biotinylated anti mouse fab fragment
    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the <t>Aβ-fibrinogen</t> interaction. (A) <t>Biotinylated</t> Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated
    Biotinylated Anti Mouse Fab Fragment, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno biotinylated f
    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the <t>Aβ-fibrinogen</t> interaction. (A) <t>Biotinylated</t> Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated
    Biotinylated F, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 90/100, based on 240 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno biotinylated anti rabbit fab fragment
    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the <t>Aβ-fibrinogen</t> interaction. (A) <t>Biotinylated</t> Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated
    Biotinylated Anti Rabbit Fab Fragment, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with mono-biotinylated fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p

    Journal: Nature Communications

    Article Title: WASP family proteins regulate the mobility of the B cell receptor during signaling activation

    doi: 10.1038/s41467-020-14335-8

    Figure Lengend Snippet: Single-particle tracking reveals wide range of BCR mobility. a Panel showing primary murine B cell spreading (IRM, above) and BCR clustering (TIRF, below). Scale bar is 3 μm. b Experimental schematic, indicating activated murine primary B cells, placed on supported lipid bilayers coated with mono-biotinylated fragments of antibody (mbFab). Cells are imaged in TIRF mode and the concentration of AF546 labeled mbFab is kept low enough to image single-molecule events. c Representative TIRF image with the bright dots representing single BCR molecules. The cell contour is obtained from an IRM image taken after TIRF imaging. Scale bar is 1 μm. d The collection of tracks obtained for a control cell during a 10-min period imaged at 33 Hz for 1000 s every minute. The tracks are color coded for diffusivity. Scale bar is 1 μm. e Cumulative distribution function (CDF) for the diffusivities measured at 1, 3, 5, 7, and 9 min after activation for BCR in B cells from control mice. f Boxplot showing BCR diffusivities at the indicated time points ( N = 15 cells). The mean is marked with red diamonds, the bottom line represents the lower quartile, the upper line the upper quartile, the whiskers show the extent of the rest of the data, and red crosses are the outliers. Significance of differences was tested using the Kruskal–Wallis test ( ***p

    Article Snippet: Mono-biotinylated fragment of antibody (mbFab′-anti-Ig) was generated from the F(ab′)2 fragment (Jackson Immuno Research, West Grove PA) using a published protocol .

    Techniques: Single-particle Tracking, Concentration Assay, Labeling, Imaging, Activation Assay, Mouse Assay

    ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic DNA (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a biotinylated Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).

    Journal: Genome Research

    Article Title: Mobile element scanning (ME-Scan) identifies thousands of novel Alu insertions in diverse human populations

    doi: 10.1101/gr.148973.112

    Figure Lengend Snippet: ME-Scan library preparation ( A–E ) and sequencing ( F–H ). ( A ) Genomic DNA (green) containing an Alu Yb8/9 (blue) in the forward orientation. The 5′ GC-rich region, the 3′ poly-A tail, and the Alu Yb8/9-specific primer site ( Alu BP2) are shown as darker segments. The target site duplications (TSD) are indicated by boxed black arrows. ( B ) DNA samples are fragmented, end-repaired, and an overhanging 3′ A is added. ( C ) Partially double-stranded oligonucleotide adapters (orange) with 9-bp indexes (darker segment) are ligated onto fragment ends. Indexed samples are then pooled. ( D ) Alu Yb8/9 element junctions are targeted by PCR using a biotinylated Alu Yb8/9-specific primer ( Alu BP2) and adapter primer PEP2. Biotinylated DNA molecules are then purified using streptavidin-coated paramagnetic beads. ( E ) Reamplification of the library with primers PEP1 and PEP2 (orange arrows). ( F–H ) The pooled junction library is then sequenced with a three-read design. Primers are shown as arrows, sequencing reads as dashed lines. The first sequencing read (50 nt) extends from Alu SPv2 ( F ) or Alu SPv3 ( G ). To skip the 5′ end of the Alu insertions, which would be identical over the entire flow cell and therefore difficult for Illumina's software to process, the first 30 cycles of nucleotide synthesis are carried out without collecting data (represented by a dashed gray ‘hop’). The second read proceeds for 57 bp from Alu SPIn1. The third read is generated using Illumina's standard second-end read primer and consists of a 9-bp index, a ‘T,’ and 36 bp of genomic sequence from a fragmentation site 50–300 bp upstream of the Alu insertion. Read sets are generated from multiple different fragments representing each Alu Yb8/9 insertion in the library ( H ). Each insertion is uniquely identified by its “ Alu Junction Position” (dashed line and large arrow in F and G ).

    Article Snippet: The size-selected DNA was incubated with streptavidin-coated paramagnetic beads to retain biotinylated DNA fragments per the manufacturer's protocol (Dynabeads MyOne Streptavidin C1, Life Technologies, Inc.).

    Techniques: Sequencing, Polymerase Chain Reaction, Purification, Flow Cytometry, Software, Generated

    Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the Aβ-fibrinogen interaction. (A) Biotinylated Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated

    Journal: Blood

    Article Title: Biochemical and structural analysis of the interaction between β-amyloid and fibrinogen

    doi: 10.1182/blood-2016-03-705228

    Figure Lengend Snippet: Naturally occurring p3 peptides, Aβ17-40 and Aβ17-42, inhibit the Aβ-fibrinogen interaction. (A) Biotinylated Aβ42 was incubated with fibrinogen in the presence of various concentrations (0.05-20 µM) of 16 nonbiotinylated

    Article Snippet: For the AlphaLISA assay, various concentrations (0.02-20 µM) of N-terminally biotinylated Aβ fragments 1 to 16, 15 to 25, 22 to 41, and 1 to 42 (50 nM, Anaspec) were incubated with 1 nM fibrinogen for 30 minutes at RT in a final volume of 10 µL of assay buffer (25 mM Tris-HCl, pH 7.4, 150 mM NaCl, 0.05% Tween-20, 0.1% BSA) in white 384-well plates (Greiner).

    Techniques: Incubation